Recombinant Human Parvalbumin Alpha (PVALB) Protein (His-SUMO)

Name: Recombinant Human Parvalbumin Alpha (PVALB) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10163P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Parvalbumin Alpha (PVALB) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P20472
Target Symbol	PVALB
Synonyms	D22S749; MGC116759; Parvalbumin alpha; PRVA_HUMAN; PVALB
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	SMTDLLNAEDIKKAVGAFSATDSFDHKKFFQMVGLKKKSADDVKKVFHMLDKDKSGFIEEDELGFILKGFSPDARDLSAKETKMLMAAGDKDGDGKIGVDEFSTLVAES
Expression Range	2-110aa
Protein Length	Full Length of Mature Protein
Mol. Weight	27.9kDa
Research Area	Metabolism
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	In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Protein Families	Parvalbumin family
Database References	HGNC: 9704 OMIM: 168890 KEGG: hsa:5816 STRING: 9606.ENSP00000216200 UniGene: Hs.295449

Gene Functions References

These results demonstrate a specific association between elevated PVALB methylation and METH-induced psychosis. PMID: 28835159
Our data support the hypothesis that the loss of PVALB plays a role in the pathogenesis of thyroid tumors. PMID: 27458244
This study showed that the density of parvalbumin was significantly diminished in the basolateral complex in patients with Parkinson Disease. PMID: 28859333
The results of this study suggested that innervation from PV-containing thalamic nuclei extends across superficial and middle layers of the human dorsolateral prefrontal cortex. PMID: 28074478
This study demonstrated that A reduction of PV-positive cells and PV-immunoreactivity was observed exclusively in FCD type I/III specimens compared with cryptogenic tissue from control patients with a poor postsurgical outcome. PMID: 27173597
excitatory synapse density is lower selectively on parvalbumin interneurons in schizophrenia and predicts the activity-dependent down-regulation of parvalbumin and GAD67 PMID: 27444795
Increased numbers of PVALB neurons and fiber labeling in focal cortical dysplasia compared to nondysplastic epileptic temporal neocortex and postmortem controls may be related to cortical malformation. PMID: 26081613
TRPV1-, TRPV2-, P2X3-, and parvalbumin-immunoreactivity neurons in the human nodose ganglion innervate the pharynx and epiglottis through the pharyngeal branch and superior laryngeal nerve PMID: 24764033
This study demonistrated that differentially expressed in PV neurons in subjects with schizophrenia, including genes associated with WNT (wingless-type), NOTCH, and PGE2 (prostaglandin E2) signaling. PMID: 24628518
This study showed that the parvalbumin basket cell inputs in the dorsolateral prefrontal cortex were lower in patient with schizophrenia. PMID: 24217255
mRNA labeling at the single cell level shows a significant decrease in parvalbumin expression in Parkinson's (PD) cases; however, neuronal density of parvalbumin-positive neurons was not significantly different between PD patients and controls. PMID: 23891794
This study demonistrated that loss of parvalbium immunoreactive axons in anterolateral columns of spinal cord in patient of lateral sclerosis spinal cords PMID: 23764361
A subpopulation of projection neurons containing calcium-binding protein parvalbumin (PV) is identified in a precise mapping of the GABAergic cortical distribution. PMID: 23254904
Parvalbumin neurons decrease the drive of the input to the visual cortex in contrast sensitivity. PMID: 23825418
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
PVALB is a novel diagnostic marker for Hurthle ademonas of the thyroid. PMID: 20926528
parvalbumin has a role in calcium handling in cardiac diastolic dysfunction [review] PMID: 20093724
In subjects with schizophrenia a reduction in parvalbumin [PV] and GAD67 mRNA expression in prefrontal cortex neurons was noted PMID: 12867516
Slow relaxation caused by alpha-Tm mutants can be corrected by modifying calcium handling with parvalbumin. PMID: 15059934
In dopaminergic cells of the substantia nigra in Parkinson disease an increased parvalbumin content is detected reflecting a natural protective mechanism against putative increase of intracellular calcium caused by excitotoxic injury and oxidative stress. PMID: 15257133
demonstration of a reduced number of parvalbumin-immunoreactive projection neurons in the mammillary bodies in schizophrenia PMID: 17405923
There is no correlation between total neuronal loss and PV-ir neuronal loss in any of the hippocampal fields in epileptic patient. PMID: 17850980
The results of this study indicate a significant reduction in the number of PV interneurons within layer 2 of the multiple sclerosis primary motor cortex PMID: 18297277
sequencing of PVALB was performed in 132 cases of Gitelman's syndrome in whom only one or no (N = 79) mutant SLC12A3 allele was found PMID: 18469313

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.