CD5L Human, HEK

CD5 Molecule-Like Human Recombinant, HEK
Cat. No.
BT30275
Source
HEK 293.
Synonyms
CD5 antigen-like, CT-2, IgM-associated peptide, SP-alpha, CD5L, API6, AIM, API6, PRO229, Spalpha.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

CD5L Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser20-Gly347) containing a total of 334 amino acids, having a calculated molecular mass of 36.9kDa and fused to a 6 aa His tag at C-Terminus.

Product Specs

Introduction
The CD5 antigen-like protein (CD5L) plays a role in regulating the immune system by acting as an apoptosis inhibitor. CD5L is found in various parts of the body, including the spleen, lymph nodes, thymus, and bone marrow.
Description
Recombinant human CD5L, produced in HEK cells, is a single glycosylated polypeptide chain with a sequence spanning from Ser20 to Gly347. This protein contains 334 amino acids, including a 6 amino acid His tag located at the C-terminus. The calculated molecular mass of the protein is 36.9 kDa.
Physical Appearance
The product is supplied as a white lyophilized (freeze-dried) powder that has been filtered.
Formulation
The CD5L protein was filtered through a 0.4 µm filter and subsequently lyophilized from a 0.5 mg/ml solution prepared using phosphate buffered saline at pH 7.5.
Solubility
To prepare a working stock solution, add deionized water to the lyophilized pellet to achieve a concentration of approximately 0.5 mg/ml, ensuring complete dissolution. Note: This product is not sterile. Before use in cell culture, the solution should be filtered using an appropriate sterile filter.
Stability
Store the lyophilized protein at -20°C. To avoid repeated freeze-thaw cycles, aliquot the reconstituted protein. Reconstituted protein can be stored at 4°C for a short period.
Purity
Purity is determined by SDS-PAGE analysis and is greater than 95.0%.
Synonyms
CD5 antigen-like, CT-2, IgM-associated peptide, SP-alpha, CD5L, API6, AIM, API6, PRO229, Spalpha.
Source
HEK 293.
Amino Acid Sequence
SPSGVRLVGG LHRCEGRVEV EQKGQWGTVC DDGWDIKDVA VLCRELGCGA ASGTPSGILY EPPAEKEQKV LIQSVSCTGT EDTLAQCEQE EVYDCSHDED AGASCENPES SFSPVPEGVR LADGPGHCKG RVEVKHQNQW YTVCQTGWSL RAAKVVCRQL GCGRAVLTQK RCNKHAYGRK PIWLSQMSCS GREATLQDCP SGPWGKNTCN HDEDTWVECE DPFDLRLVGG DNLCSGRLEV LHKGVWGSVC DDNWGEKEDQ VVCKQLGCGK SLSPSFRDRK CYGPGVGRIW LDNVRCSGEE QSLEQCQHRF WGFHDCTHQE DVAVICSGHH HHHH.

Product Science Overview

Introduction

The CD5 molecule-like protein, also known as CD5L or CD5 antigen-like, is a member of the scavenger receptor cysteine-rich (SRCR) superfamily. This protein is expressed in various immune cells and plays a crucial role in the regulation of the immune system.

Structure and Expression

CD5L is a soluble glycoprotein that contains three SRCR domains. It is primarily expressed by macrophages in lymphoid tissues such as the spleen, lymph nodes, thymus, and bone marrow . The recombinant form of this protein, produced in HEK293 cells, consists of a single, glycosylated polypeptide chain with a calculated molecular mass of approximately 36.9 kDa .

Function

CD5L functions as a pattern recognition molecule, binding to both lipoteichoic acid (LTA) on Gram-positive bacteria and lipopolysaccharide (LPS) on Gram-negative bacteria . This binding activity is retained in the SRCR domain 1 of CD5L. The protein plays a significant role in the innate and adaptive immune systems by recognizing and responding to microbial components.

Applications

Recombinant CD5L protein is used in various research applications, including studies on immune response, cell signaling, and disease mechanisms. The protein’s ability to bind to microbial components makes it a valuable tool for investigating host-pathogen interactions and the immune system’s response to infections.

Production and Purification

The recombinant human CD5L protein is produced in HEK293 cells and purified to a high degree of purity, typically greater than 95% as determined by SDS-PAGE and SEC-HPLC . The protein is lyophilized from a sterile PBS solution and can be reconstituted for use in various experimental applications. It is recommended to store the protein under sterile conditions at -20°C to -80°C to maintain its stability and avoid repeated freeze-thaw cycles .

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