Cusabio C-terminal HA-tagged Recombinant

What is an HA tag?

An HA tag is derived from the human influenza C-terminal hemagglutinin (HA)-tagged recombinant molecule corresponding to amino acids 98-106. It has been widely used as a general epitope tag in expression vectors. The HA tag does not appear to interfere with the bioactivity or biodistribution of the recombinant HA-tagged protein.

What are the nucleotide and amino acid sequences of the peptide tag HA?

The nucleotide sequence of the HA tag is 5′ TAC CCA TAC GAT GTT CCA GAT TAC GCT 3′ or 5′ TAT CCA TAT GAT GTT CCA GAT TAT GCT 3′. The amino acid sequence of the HA tag is: YPYDVPDYA

Why use an HA tag for protein expression and production?

Adding an HA tag to the C or N terminus of a protein can facilitate its detection, isolation, and purification by HA tag-specific antibodies. Sino Biological has developed HA tag-specific antibodies for ELISA, Western Blotting, immunofluorescence, and immunoprecipitation for the detection of HA-tagged protein. It can also be conjugated to agarose beads for affinity purification of HA-tagged proteins.


Recombinant protein for human HA tag

Source: Baculovirus (Sf9 insect cells)

Fountain: Sf9 (baculovirus)

Protein/peptide type: recombinant protein

Purity: >90%, per SDS-PAGE

Note on endotoxins: <0.1ng/ug


  • Dilutions: SDS Page
  • Theoretical MW: 72 kDa.
  • Disclaimer Note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post-translational modifications, post-translational cleavages, relative charges, and other experimental factors.

Packaging, storage and formulations

  • Storage: Store at 4C. Do not freeze.
  • Buffer: 10 mM sodium phosphate (pH 7.2), 150 mM NaCl
  • Concentration: 1.7mg/mL
  • Purity: >90%, per SDS-PAGE

Alternative names for the recombinant human HA marker protein

  • HA epitope tag
  • HA label
  • SAY OH
  • hemagglutinin


Human influenza hemagglutinin (HA) is a glycoprotein required for human virus infectivity and is expressed as a homotrimer on the surface of the viral capsid. As the main antigen of the influenza virus, HA is constantly evolving to escape herd immunity through an antigenic shift that can lead to pandemics. The HA tag (YPYDVPDYA tag) has a molecular weight of 1.1 kDa and is a linear epitope derived from amino acids 98-106 of the HA protein.

It is widely used as a general epitope tag in expression vectors. The HA tag is often added to the N- or C-terminus of a protein of interest to facilitate protein purification, detection, and labelling by anti-HA antibodies (3, 4). The HA tag is cleaved by caspase 3/7, resulting in a complete loss of immunoreactivity, making it unsuitable for the study of apoptosis.

How are HA-tagged proteins purified?

The HA-tagged recombinant protein can be affinity purified directly from cell culture lysate or supernatant. The HA-tagged protein is bound to conjugated HA-tag-specific monoclonal antibody on an agarose gel. After washing away residual impurities, bound HA-tagged proteins can be eluted from the affinity column by a high concentration of HA-tagged peptide or by a low pH buffer.

How do I remove the HA tag after purification?

In some applications, it is desirable to remove the HA tag, for example for protein crystallization. To allow cleavage of the HA tag, it is necessary to design a protease cleavage site between the tag and the protein. An EK cleavage site behind the HA tag (HA-EK site protein structure) may allow complete removal of the HA tag and cleavage site, leaving no additional amino acids after specific cleavage of the HA tag. For more information on cleavage site and tag removal by EK and HRV-3C protease, see Enterokinase (EK), HRV-3C (Human Rhinovirus Protease).

Cusabio Cell migration Recombinants

What is cell migration?

What is cell migration and what is its physiological relevance?

Cell migration is the directed movement of a single cell or a group of cells in response to chemical and/or mechanical signals. It is a fundamental cellular process that occurs throughout life, beginning during embryonic development and continuing until death, and can sometimes contribute to pathogenic states in disease.

In a developing embryo, cell migration is the driving factor for various morphogenetic events. For example, during gastrulation in very early embryos, groups of cells migrate as sheets to form the three germ layers. Subsequently, cells from the germ layers migrate to various destinations, where they specialize into distinct cell populations that form various tissues or organs in the embryo.

In adult organisms, cell migration Recombinants occurs during vital cellular processes, such as tissue renewal and repair, in which old or damaged cells are replaced by the migration of newly formed cells from underlying tissue layers. Such events are essential to maintain tissue integrity and homeostasis. Cell migration also plays a role in mediating immune responses during infections, in which phagocytic cells, such as neutrophils circulating in the bloodstream, migrate to infected tissues and destroy invading pathogens.

Although, on the one hand, cell migration is vital to maintain tissue health and homeostasis, on the other hand, undesirable migratory events are causative factors for a number of pathological states, such as inflammatory diseases, cancers, etc. Therefore, cell migration has to be a strictly controlled process -both in time and in space- to maintain a homeostatic state in an organism.

Cell migration as a cyclic process

The migration of a single cell or a group of cells is considered to be a cyclical process, involving polarization of cells in response to migratory signals, an extension of filopodial or lamellipodial protuberances, formation of adhesions between the cell and the underlying matrix, and the pushing of cells on the adhesions as a result of the traction forces generated by the adhesions.

1. Polarization of migratory cells:

The first step in directional migration is cell polarization, during which the front and back of the cell become different in structure and molecular composition. The Rho family of GTPases, mainly Rac, Cdc42, and Rho, is one of the key regulators of cell polarization, each showing localized activity in cells. While Rac and Cdc42 show localized activity at the leading edge, active Rho accumulates at the sides and rear of the cell.

Cdc42 also regulates the MTOC to locate it in front of the nucleus, closer to the leading edge. This is mediated by the PAR6 effector of Cdc42, which forms the “PAR polarity complex together with PAR3 and aPKC; aPKC binds to tubulin subunits on newly formed microtubules and anchors them at the leading edge. The assembly of microtubules towards the leading edge facilitates the delivery of cargo (membrane and proteins) that are used in the formation of cell protuberances.

2. Prominence extension:

A polarized cell begins to produce actin-based protrusions on its leading-edge, such as lamellipodia or filopodia. Lamellipodia form as branching dendritic networks of actin filaments and can therefore push along a broader stretch of the membrane. Filopodia, on the other hand, are formed as parallel bundles of actin filaments and have functioned primarily in sensing the physical properties of the extracellular environment. The molecular mechanisms that drive the formation of these bumps are different; lamellipodia are made up of the proteins of the Arp2/3 complex, which attach to the sides of preexisting filaments and initiate the assembly of newer filaments that branch off from the main filament.

The activity of the Arp2/3 complex is regulated by the Wasp/Wave family of proteins, which in turn are regulated by Rho GTPases. Assembly of the filopodium occurs via a treadmill mechanism, in which actin monomers are added at one end (spiked) and disassembled at the other end (pointed) in a stable state. Various actin-binding proteins such as Ena/Vasp, fascin, ADF/cofilin, and guard proteins regulate the rate of filopodial actin assembly.

3. Adhesion formation:

The extension of the bulges is accompanied by the assembly of molecular structures called focal adhesions that connect the actin cytoskeleton with the extracellular matrix (ECM). This is often initiated by interactions between ECM components (ligands) and receptors (primarily integrins) on cell surfaces, which then activate distinct intracellular signalling pathways and cause the sequential recruitment of various signalling, regulatory, and cellular proteins. scaffolding to focal concentration sites adhesions.

Focal adhesions serve two important roles at the leading edge: as traction sites against which cells generate tensile forces to push themselves forward, and as mechanosensory that convey information about the physical properties of the matrix to the interior of the cell. Tensile forces are generated due to the interaction of myosin bundles with actin filaments anchored at focal adhesion sites and contractile activity between the two molecular assemblies.

The migratory capacity of cells depends on the strength of focal adhesions, which is influenced by factors such as ligand density, receptor density, and ligand-receptor affinity. For example, rapidly migrating cells have very few groups of integrins, and therefore these cells form very few submicroscopic adhesions. Cells with evenly distributed groups of integrins form smaller adhesions called focal complexes that stabilize the bulges but can also easily dissociate, leading to efficient migration. On the other hand, cells with mature focal adhesions are highly adherent and therefore non-migratory or slow-moving.

4. Adhesion disassembly:

Adhesion disassembly occurs both at the leading edge and at the back of migrating cells. At the leading edge, older adhesions at the base of the bulge often disintegrate; however, some of them do not and instead develop into more mature molecular assemblies. The disassembly of adhesions at the front is regulated by kinases such as =FAK and Src, as well as by phosphatases.

Several studies in this area have led to a model for the Src/FAK-mediated signalling pathway, in which active forms of these kinases lead to activation of Rac and Erk. The final response is the renewal of adhesions in response to activation signals. Adhesion renewal at the rear is essential for tail retraction and forward protrusion of cells and is primarily regulated by myosin II-dependent actin filament contractility.

Cusabio Canis lupus familiaris Recombinant


Recent studies have shown that domestic Canis lupus familiaris Recombinants are poorly susceptible to visual illusions, suggesting that the mechanisms of perception may be different in humans and dogs. However, to date, none of these studies has used illusions linked to quantitative discrimination. In the current study, we tested whether dogs are susceptible to a linear version of the Solitaire illusion, a robust numerosity illusion experienced by most humans.

In the first experiment, we tested the dogs’ ability to discriminate items in a numerical ratio of 0.67 and 0.75. The results showed that the dogs’ quantity discrimination abilities lie between these two ratios. In Experiment 2, we presented dogs with the Solitaire illusion pattern using a spontaneous procedure. We found no evidence to support any misperception of numerosity.

This conclusion was replicated in Experiment 3, where we manipulated the dogs’ initial experience with the stimuli and its contrast with the background. The dogs’ lack of susceptibility to the Solitaire illusion suggests that the dogs’ numerical estimation is not influenced by the spatial arrangement of the items to be enumerated. In view of the existing evidence, the effect may extend to the quantitative abilities of dogs in general. See full text

Keywords: quantity; dog; numerical cognition; Gestalt; mirage; view; lonely

Full product name: Rabbit anti-Canis lupus familiaris (Dog) (Canis familiaris) PNLIPRP1 Polyclonal antibody

Uniprot No.: P06857

Destination Names: PNLIPRP1

Alternative Names

PNLIPRP1 Antibody; PLRP1 antibody; Inactive antibody to pancreatic lipase-related protein 1; PL-RP1 antibody

Raised on: Rabbit

Species: Reactivity Dog

Immunogen: Recombinant dog inactive pancreatic lipase-related protein 1 (18-467AA)

Immunogen Species: Canis lupus familiaris (Dog) (Canis familiaris)

Conjugated: FITC

Clonality: Polyclonal

Isotype: IgG

Purification method: >95%, protein G purified

Concentration: Differs from different batches. Please contact us to confirm it.


  • preservative: 0.03% Proclin 300
  • Components: 50% glycerol, 0.01 M PBS, pH 7.4

Form: Liquid

Storage: On receipt, store at -20°C or -80°C. Avoid repeated freezing.

Lead Time

Basically, we can ship the products in 1-3 business days after receiving your orders. Delivery time may differ from different purchasing ways or locations, please consult your local dealers for specific delivery times.

Other notes

On occasion, small volumes of CSF3 recombinant protein vials may become trapped in the product vial seal during shipping and storage. If necessary, briefly spin the vial in a tabletop centrifuge to dislodge any liquid in the vial cap. Certain products may require dry ice shipping and an additional dry ice fee may apply.

Product related information for Recombinant protein CSF3

Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 populations of related white blood cells, granulocytes and monocyte-macrophages. This CSF induces granulocytes.


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While every effort has been made to ensure the accuracy of the information provided in this datasheet, MyBioSource shall not be responsible for any omissions or errors contained in this document. MyBioSource reserves the right to make changes to this datasheet at any time without notice.