Migration Assay: Cells expressing recombinant CCR1 were assayed for migration through a transwell filter at various concentrations of WT or Biotinylated HCC-1. Responses are expressed as the % of total input cells (Blue: wild type; Red: biotinylated).

Biotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14) 8021

Price range: $134.00 through $3,368.00

Summary

Expression: E.coli
Amino Acid Range: 28-93

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SKU: 8021parent Categories: chemokine, proteins Tag: CCL14 (HCC-1)

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P16627
express system	E.coli
product tag	biotin at C-terminal
purity	> 97% by SDS PAGE
molecular weight	Predicted Molecular Mass: 10,219.5471 Da Extinction Coefficient: 19,300 M-1 cm-1 Actual Molecular Mass: 10,219.5471 Da by ESI Mass Spec
available size	10 µg, 100 µg, 2 µg, 50 µg
endotoxin	<0.01 EU per 1μg of the protein by the LAL method

Biotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14) 8021

protein
Database link: human P16627
Size and concentration 2, 10, 50, 100µg and lyophilized
Form Lyophilized
Storage Instructions Avoid repeated freeze-thaw cycles: • 12 months from date of receipt, -20 to -70 °C as supplied. • 1 month, 2 to 8 °C under sterile conditions after reconstitution. • 3 months, -20 to -70 °C under sterile conditions after reconstitution
Storage buffer Ã¢â‚¬â€¹Reconstitution: Spin sample prior to reconstitution. Recommended concentration of 100µg/mL in sterile water. Shipping: Room Temp
Purity > 97% by SDS PAGE and HPLC

target relevance
Hemofiltrate CC chemokine-1(HCC-1/CCL14) is endogeneously expressed by numerous tissues. Upon processing of the N terminal residues of the full length HCC-1 by the uPA-plasmin system, the active form of HCC-1 is a strong agonist for CCR1, CCR5 and to a lesser extent CCR3, and causes chemotaxis of different types of leukocytes. The active form of HCC-1 is also shown as a potent inhibitor of HIV entry.
Protein names Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa-like protein 1) (Spermatid-specific heat shock protein 70)
Gene names Hspa1l,Hspa1l Hsc70t
Protein family Heat shock protein 70 family
Mass 70637Da
Function FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria. {ECO:0000250\|UniProtKB:P34931}.
Tissues TISSUE SPECIFICITY: Expressed in spermatids.
Structure SUBUNIT: Interacts with PRKN. {ECO:0000250\|UniProtKB:P34931}.
Domain DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. {ECO:0000250\|UniProtKB:P34931}.
Target Relevance information above includes information from UniProt accession: P16627
The UniProt Consortium

Data

Migration Assay: Cells expressing recombinant CCR1 were assayed for migration through a transwell filter at various concentrations of WT or Biotinylated HCC-1. Responses are expressed as the % of total input cells (Blue: wild type; Red: biotinylated).

FAQ & Publications

Frequently Asked Questions

What is the expression system used for producing Biotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14)?

The Biotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14) is expressed using an Escherichia coli (E.coli) expression system.

How should I store the lyophilized Biotinylated HCC-1 protein to maintain its stability?

The lyophilized protein should be stored at -20 to -70 °C as supplied, which preserves stability for up to 12 months. After reconstitution, it can be stored for 1 month at 2 to 8 °C under sterile conditions or for 3 months at -20 to -70 °C under sterile conditions. Avoid repeated freeze-thaw cycles to maintain protein integrity.

What is the purity level of this Biotinylated HCC-1 protein preparation?

The Biotinylated HCC-1 protein preparation has a purity greater than 97% as determined by SDS-PAGE and HPLC analysis.

Is the Biotinylated HCC-1 protein endotoxin-free, and how is this measured?

Yes, the endotoxin level is less than 0.01 endotoxin units (EU) per microgram of protein, as measured by the Limulus Amebocyte Lysate (LAL) assay method.

What biological activities are associated with the active form of HCC-1 after N-terminal processing?

The active form of HCC-1, generated by N-terminal processing via the uPA-plasmin system, is a potent agonist for chemokine receptors CCR1, CCR5, and to a lesser extent CCR3. It induces chemotaxis of various leukocyte types and has been shown to inhibit HIV entry effectively.

Publications

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We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from the PubMed database provided by the United States National Library of Medicine at the National Institutes of Health.