Recombinant Human Calbindin (CALB1) Protein (His)

Name: Recombinant Human Calbindin (CALB1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00508P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Calbindin (CALB1) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P05937
Target Symbol	CALB1
Synonyms	(Calbindin D28)(D-28K)(Vitamin D-dependent calcium-binding protein, avian-type)
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	C-6His
Target Protein Sequence	AESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELQQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQDLDINNITTYKKNIMALSDGGKLYRTDLALILCAGDN
Expression Range	2-261aa
Protein Length	Full Length of Mature Protein
Mol. Weight	30.8 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
Protein Families	Calbindin family
Database References	HGNC: 1434 OMIM: 114050 KEGG: hsa:793 STRING: 9606.ENSP00000265431 UniGene: Hs.65425

Gene Functions References

CSF calbindin concentration is a sensitive biomarker of NPC1 disease PMID: 27307499
We identified a significant association between the A allele of rs1805874 and the risk of Parkinson's disease (OR 1.257, 95% CI 1.036-1.524, p = 0.020). Our findings suggest that the A allele of rs1805874 is associated with risk of Parkinson's disease among the Han Chinese. Our results, combined with previous studies, suggest that rs1805874 is associated with Parkinson's disease in East Asians, but not Caucasians. PMID: 27611799
Age-related loss of CB appears to coincide with tangle formation in the BFCN and is associated with the full range of tau pathology, including late appearing epitopes. PMID: 26417681
Increased number of calbindin neurons and fiber labeling both in focal cortical dysplasia (FCD) and non-FCD specimens compared with postmortem controls may be associated with ongoing seizure activity. PMID: 26081613
expressed by different neuron types, both inhibitory (GABAergic) and excitatory (glutamatergic), involved in both intrinsic and extrinsic circuits of the human cerebellar cortex PMID: 24719368
The calbindin-D 28k was decreased in the putamen, the dorsal tier of the substantia nigra along the lower border of the red nucleus, and in the cerebellar cortex in multiple system atrophy. PMID: 23715974
Significantly reduced hippocampal calbindin D28K levels are found in all patients with mitochondrial encephalomyopathy, lactic acidosis and stroke-like syndrome (MELAS). PMID: 22483853
Data show calbindin (CB)- and tyrosine hydroxylase (TH)-cells were distributed in the three striatal territories, and the density of calretinin (CR) and parvalbumin (PV) interneurons were more abundant in the associative and sensorimotor striatum. PMID: 22272358
Dynamics of Ca2+ ions within the solvation shell of calbindin D9k. PMID: 21364983
upregulated in endometriosis tissues PMID: 20452033
cultured syncytiotrophoblast cells express calbindin-D9k and calbindin-D28k genes, which are stimulated by calcitriol PMID: 20214988
Our study shows there is no association between rs1805874 and risk for Parkinson's disease (PD) in four Caucasian populations. This suggests the effect of calbindin on PD risk displays population specificity. PMID: 19674066
calbindin may play a role in development of Purkinje cells located in heterotopias and cerebellar dysgenesias PMID: 20054781
S-nitrosation of Ca(2+)-loaded and Ca(2+)-free recombinant calbindin D(28K) from human brain. PMID: 11994015
binds to myo-inositol-1(or 4)-monophosphatase (IMPase) and increases the phosphatase activity PMID: 12176979
calbindin 1, 28kDa may play a role in Ca2+ transport or cell development in human trophoblast possibly trough Ca2+ buffering PMID: 12606474
The biological function of calbindin D28k appears to be tied to the redox state of its five cysteine residues. PMID: 15641794
Post-translational modifications of human calbindin. PMID: 15741335
Our findings indicate that the expression of parvalbumin or calbindin-D(28k) by subpopulations of dysplastic neurons in cortical tubers is aberrant and denotes dysfunctional inhibitory circuits inept for excitoprotection. PMID: 17156698
aggregates of mutant ataxin-l may recruit calbindin-D28k via tissue transglutaminase 2 mediated covalent crosslinking PMID: 17442486
recombinant human calbindin-D28k was crystallized at 291 K using PEG 3350 as precipitant and a 2.4 A resolution X-ray data set was collected from a single flash-cooled crystal PMID: 18259068
calbindin D(28k) binds Zn2+ to 3 rather strong sites with dissociation constants in low micromolar range. Zn2+-bound state is structurally distinct from Ca2+-bound state, with negative allosteric interaction between Zn- & Ca-binding events. PMID: 18359862
CALB1 is associated with Parkinson's disease independently of alpha-synuclein. PMID: 18568448
No significant differences in cerebellar Purkinje cells in levels of CALB in autism or in the normal cerebellum. PMID: 18587625

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.