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immunoglobulin light chain variable region fragment [Homo sapiens] Catalog No.GP10100

Immunoglobulin light chain fragment

Size Price Stock Qty
1mg
$34.00
In stock
5mg
$103.00
In stock
10mg
$186.00
In stock
25mg
$256.00
In stock

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Sample solution is provided at 25 µL, 10mM.

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Chemical Properties

Cas No. N/A SDF
Synonyms H2N-Phe-Thr-Leu-Lys-Ile-Ser-Arg-OH
Chemical Name N/A
Canonical SMILES NC(C(NC(C(C)O)C(NC(CC(C)C)C(NC(CCCCN)C(NC(C(C)CC)C(NC(CO)C(NC(CCCNC(N)=N)C(O)=O)=O)=O)=O)=O)=O)=O)CC1=CC=CC=C1
Formula C40H69N11O10 M.Wt 864.04
Solubility ≥ 86.4mg/mL in DMSO Storage Store at -20°C
General tips For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
Shipping Condition Evaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request
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Background

Immunoglobulin light chain variable region fragment [Homo sapiens] is a fragment (Phe-Thr-Leu-Lys-Ile-Ser-Arg) on the variable region of the human immunoglobulin light chain.

Immunoglobulins (Ig) are the antigen recognition molecules of B cells. An Ig molecule is made up of 2 identical heavy chains and 2 identical light chains joined by disulfide bonds so that each heavy chain is linked to a light chain and the 2 heavy chains are linked together. On each of the light chain, there is one variable region and a constant region. The variable region is the most important for binding to antigens.

The antigen combining site of an antibody is made up of the variable regions of one light chain and one heavy chain. Within the variable regions, typically comprising 105-110 amino acids, some positions show more sequence variation than others. The variable fragments are the smallest fragment made from enzymatic cleavage of IgG and IgM class antibodies.

References:
1. Janeway CA, Jr et al. (2001). Immunobiology. (5th ed.). Garland Publishing. ISBN 0-8153-3642-X
2. Woof J, Burton D (2004). "Human antibody-Fc receptor interactions illuminated by crystal structures". Nat Rev Immunol 4 (2): 89–99. doi :10.1038/nri1266. PMID 15040582.
3. Mattu T, Pleass R, Willis A, Kilian M, Wormald M, Lellouch A, Rudd P, Woof J, Dwek R (1998). "The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions". J Biol Chem 273 (4): 2260–72. doi:10.1074/jbc.273.4.2260. PMID 9442070.
4. Roux K (1999). "Immunoglobulin structure and function as revealed by electron microscopy". Int Arch Allergy Immunol 120 (2): 85–99. doi :10.1159/000024226. PMID 10545762.
5. Barclay A (2003). "Membrane proteins with immunoglobulin-like domains–a master superfamily of interaction molecules". Semin Immunol 15 (4): 215–23. doi :10.1016/S1044-5323(03)00047-2. PMID 14690046 .
6. Putnam FW, Liu YS, Low TL (1979). "Primary structure of a human IgA1 immunoglobulin. IV. Streptococcal IgA1 protease, digestion, Fab and Fc fragments, and the complete amino acid sequence of the alpha 1 heavy chain". J Biol Chem 254 (8): 2865–74. PMID 107164.
7. Huber R (1980). "Spatial structure of immunoglobulin molecules". Klin Wochenschr 58 (22): 1217–31. doi :10.1007/ BF01478928 6780722.