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SDS-PAGE

CHL-1 recombinant protein

Recombinant Human CHL-1 Protein (His tag)

Gene Names
CHL1; CALL; L1CAM2
Purity
> 95 % as determined by SDS-PAGE
Synonyms
CHL-1; Recombinant Human CHL-1 Protein (His tag); CALL; FLJ44930; L1CAM2; MGC132578; CHL-1 recombinant protein
Ordering
For Research Use Only!
Host
Human Cells
Purity/Purification
> 95 % as determined by SDS-PAGE
Form/Format
Lyophilized from sterile PBS, pH 7.4
Sequence Length
1208
Application Notes
The recombinant human CHL1 consists of 1067 amino acids after removal of the signal peptide and predicts a molecular mass of 120 kDa. As a result of glycosylation, the apparent molecular mass of rhCHL1 is approximately 160-180 kDa in SDS-PAGE under non-reduced conditions.
Predicted N Terminal
Ile 25
Endotoxin
< 1.0 EU per mug of the protein as determined by the LAL method
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

SDS-PAGE
Related Product Information for CHL-1 recombinant protein
Background: Neural cell adhesion molecule L1-like protein, also known as close homolog of L1 (CHL1) is the prototypic member of the CTF / NF-1 family of transcription factors that serve as a novel calcium signaling pathway-responsive transcription factor and is considered as a member of the largest ctf complementation group, consisting of 30 of 126 ctf mutants isolated. CHL1 is a cell adhesion molecule highly related to L1. It contains structure plan of six extracellular C2-type immunoglobulin (Ig) domains followed by five fibronectin type III domains linked by a single membrane-spanning region to a short cytoplasmic domain. The extracellular portion of CHL1 is higyly glycosylated and involved them in hemophilic disease.

Description: A DNA sequence encoding the extracellular domain of human CHL1 (AAI04919.1) (Met 1-Gln 1080) was fused with a polyhistidine tag at the C-terminus.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
Molecular Weight
136,698 Da
NCBI Official Full Name
CHL1 protein
NCBI Official Synonym Full Names
cell adhesion molecule L1 like
NCBI Official Symbol
CHL1
NCBI Official Synonym Symbols
CALL; L1CAM2
NCBI Protein Information
neural cell adhesion molecule L1-like protein
UniProt Protein Name
Neural cell adhesion molecule L1-like protein
UniProt Gene Name
CHL1
UniProt Synonym Gene Names
CALL

NCBI Description

The protein encoded by this gene is a member of the L1 gene family of neural cell adhesion molecules. It is a neural recognition molecule that may be involved in signal transduction pathways. The deletion of one copy of this gene may be responsible for mental defects in patients with 3p- syndrome. This protein may also play a role in the growth of certain cancers. Alternate splicing results in both coding and non-coding variants. [provided by RefSeq, Nov 2011]

Uniprot Description

CHL1: Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons and in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane. Belongs to the immunoglobulin superfamily. L1/neurofascin/NgCAM family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Cell adhesion; Cell development/differentiation; Extracellular matrix; Membrane protein, integral; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 3p26.3

Biological Process: signal transduction

Research Articles on CHL-1

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Product Notes

The CHL-1 chl1 (Catalog #AAA2546488) is a Recombinant Protein produced from Human Cells and is intended for research purposes only. The product is available for immediate purchase. The recombinant human CHL1 consists of 1067 amino acids after removal of the signal peptide and predicts a molecular mass of 120 kDa. As a result of glycosylation, the apparent molecular mass of rhCHL1 is approximately 160-180 kDa in SDS-PAGE under non-reduced conditions. Researchers should empirically determine the suitability of the CHL-1 chl1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "CHL-1, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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