Recombinant Human Secreted Ly-6/Upar-Related Protein 1 (SLURP1)

Name: Recombinant Human Secreted Ly-6/Upar-Related Protein 1 (SLURP1)
Brand: Beta LifeScience
SKU: BLC-08046P
Availability: InStock

Greater than 85% 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 Secreted Ly-6/Upar-Related Protein 1 (SLURP1) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P55000
Target Symbol	SLURP1
Synonyms	SLURP1; ARS; Secreted Ly-6/uPAR-related protein 1; SLURP-1; ARS component B; ARS(component B)-81/S; Anti-neoplastic urinary protein; ANUP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	LKCYTCKEPMTSASCRTITRCKPEDTACMTTLVTVEAEYPFNQSPVVTRSCSSSCVATDPDSIGAAHLIFCCFRDLCNSEL
Expression Range	23-103aa
Protein Length	Full Length of Mature Protein
Mol. Weight	8.9 kDa
Research Area	Cardiovascular
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	Has an antitumor activity. Was found to be a marker of late differentiation of the skin. Implicated in maintaining the physiological and structural integrity of the keratinocyte layers of the skin. In vitro down-regulates keratinocyte proliferation; the function may involve the proposed role as modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-7-dependent nAChR currents in an allosteric manner. In T cells may be involved in regulation of intracellular Ca(2+) signaling. Seems to have an immunomodulatory function in the cornea. The function may implicate a possible role as a scavenger receptor for PLAU thereby blocking PLAU-dependent functions of PLAUR such as in cell migration and proliferation.
Subcellular Location	Secreted.
Database References	HGNC: 18746 OMIM: 248300 KEGG: hsa:57152 STRING: 9606.ENSP00000246515 UniGene: Hs.103505
Associated Diseases	Mal de Meleda (MDM)
Tissue Specificity	Granulocytes. Expressed in skin. Predominantly expressed in the granular layer of skin, notably the acrosyringium. Identified in several biological fluids such as sweat, saliva, tears, plasma and urine.

Gene Functions References

These findings strongly suggest that down regulation of SLURP1 expression may be implicated in the pathogenesis of various solid tumors, particularly malignancies of squamous lineage, and thus this gene may be a squamous lineage-specific tumor suppressor. PMID: 29231248
This is the first mal de Meleda case of Javanese ethnicity to be documented, and the unique mutation has not previously been reported. PMID: 29023701
We identified a mutation in SLURP1 in five members of a consanguineous family in Pakistan, who had Mal de Meleda. PMID: 29226984
novel splice site mutation c.58+5G>T in mal de Meleda in India PMID: 26254200
Results of this study suggest understand Mal de Meleda, it will be important to identify proteins that interact with mutatated SLURP1. In any such studies, it will be important to assess binding of mutant SLURP1 proteins that cause Mal de Meleda. PMID: 25919322
To our knowledge, the present study is the fi rst report on molecular investigation of Mal de Meleda from Libya. PMID: 24738704
This supports the hypothesis that the antiproliferative activity of SLURP-1 is related to 'metabotropic' signaling pathway through alpha7-nAChR, that activates intracellular signaling cascades without opening the receptor channel. PMID: 26905431
SLURP1 participates in pathophysiology of psoriasis by regulating keratinocyte proliferation and differentiation, and by suppressing the growth of S. aureus PMID: 26474319
Palmoplantar keratoderma of the Gamborg-Nielsen type is caused by mutations in the SLURP1 gene and represents a variant of Mal de Meleda. PMID: 24604124
rSLURP-1 decreased production of TNFalpha by T-cells, downregulated IL-1 beta and IL-6 secretion by macrophages, and moderately upregulated IL-10 production by both types of immunocytes PMID: 24877120
This report further expands the spectrum of clinical phenotypes associated with mutations in SLURP1 in the Mediterranean population. PMID: 24093092
mutations in SLURP1 as a cause for mal de Meleda and suggest an ancient founder effect for p.W15R in the western European population. PMID: 23290002
Those findings suggested that SLURP-1 and stimulus through alpha7 nicotinic ACh receptors actively controlled asthmatic condition by stimulating ciliary beating and also by suppressing airway inflammation. PMID: 23876317
The pro-oncogenic effects of tobacco nitrosamine (4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone) can be abolished, in part, by rSLURP-1 that also upregulated RUNX3. PMID: 22369755
Patients with Mal de Meleda with the homozygous SLURP-1 G86R mutation may have an impaired T-cell activation PMID: 20854438
Results indicate that activation of alpha(7)-nAChR by SLURP-1 leads to upregulation of NF-kappaB gene expression due to activation of the Raf-1/MEK1/ERK1/2 cascade that proceeds via two complementary signaling pathways. PMID: 20660165
These findings suggest that SLURP-1 may play an important role in the control and maintenance of the periodontal ligament by protecting the periodontal ligament fibroblasts from apoptosis. PMID: 20337899
Those findings suggest that diminished expression of SLURP-1 in asthma attenuates its negative regulation of airway inflammation, and that perhaps changes in SLURP-1 expression could serve as a marker of airway damage in asthma. PMID: 20621062
Our findings indicate that the MDM type of transgressive PPK is caused by SLURP-1 mutations in patients from various origins and demonstrate allelic heterogeneity for mutations in SLURP-1. PMID: 12483299
Novel mutations in the gene encoding protein-SLURP-1 and 5 haplotypes in Mal de Meleda. Founder mutation, conserved cysteine residue to tyrosine (C99Y), in inbred pedigree, and a signal sequence mutation (W15R), homozygous and heterozygous. PMID: 12603845
Recurrent nonsense mutation, R96X, in four families of Turkish descent. These families share common ancestral haplotype at mal de Meleda locus, suggesting founder effect. PMID: 12787122
Identification of SLURP1 as an epidermal neurotransmitter explains the clinical phenotype of Mal de Meleda. PMID: 14506129
ARS Component B and its protein product SLURP1 are implicated in maintaining the physiological and structural integrity of the keratinocyte layers of the skin. PMID: 14721776
Mutation analysis revealed a homozygous missense mutation (G86R) in exon 3 of ARS gene of this patient PMID: 15909066
Biological role of SLURP-1 in the epidermis is to provide fine tuning of the physiologic regulation of keratinocyt functions through the cholinergic pathways. PMID: 16354194
anti-tumorigenic activities of SLURP-1 and -2 were demonstrated both in vitro and in vivo. PMID: 17643396
SLURP-1 participates in the regulation of gut immune functions and motility, as well as possibly playing a role in colon carcinogenesis/cancer progression. PMID: 18764860
these results expand the spectrum of mutations in SLURP-1 gene. PMID: 19692209

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.