Human Integrin alpha 6 beta 4 (ITGA6&ITGB4) Heterodimer Protein, His Tag&Tag Free, low endotoxin (MALS verified)

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IN4-H52W3-100ug
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Synonyms

Integrin alpha 6 beta 4, ITGA6&ITGB4

Source

Human ITGA6&ITGB4 Heterodimer Protein, His Tag&Tag Free (IN4-H52W3) is expressed from human 293 cells (HEK293). It contains AA Phe 24 - Gly 1012 | Asn 28 - Ser 710 (Accession # P23229-2 & P16144-2).

Predicted N-terminus: Phe 24 | Asn 28

Molecular Characterization

Human ITGA6&ITGB4 Heterodimer Protein, His Tag&Tag Free, produced by co-expression of ITGA6 and ITGB4, has a calculated MW of 116.8 kDa (ITGA6) and 81.8 kDa (ITGB4). Subunit ITGA6 is fused with an acidic tail at the C-terminus and followed by a polyhistidine tag and subunit ITGB4 contains no tag but a basic tail at the C-terminus. The non-reducing (NR) protein migrates as 130-140 kDa (ITGA6) and 75-85 kDa (ITGB4) when calibrated against Star Ribbon Pre-stained Protein Marker respectively due to glycosylation.

The protein is designed as a heterodimer.

Endotoxin

Less than 0.01 EU per μg by the LAL method / rFC method.

Purity

>95% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

Formulation

Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, 0.2 M Arginine, pH7.5 with trehalose as protectant.

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Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Shipping and Storage

This product is shipped at ambient temperature.

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

Background

Human integrin alpha(10)I domain as a recombinant protein to reveal its ligand binding specificity. In general, alpha(10)I did recognize collagen types I-VI and laminin-1 in a Mg(2+)-dependent manner, whereas its binding to tenascin was only slightly better than to albumin. Alpha 10 beta 1 is a known collagen-binding I domain integrin, in addition to α1β1, α2β1 and α11β1. GROGER found in the N-terminal domain of collagens I and III, is only weakly recognised by α10β1, an important collagen receptor on chondrocytes, contrasting with the other collagen-binding integrins.