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Description:

Interleukin-22 Human Recombinant, Sf9

IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

Product # :

CYT-1092

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Description

IL22 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (34-179 a.a.) fused to a 6 aa His Tag at C-terminus containing a total of 155 amino acids and having a molecular mass of 17.8kDa. IL22 is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL22 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to induce IL-10 secretion using COLO 205 human colorectal adenocarcinoma cell is ≤ 1.2 ng/ml.

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Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10R? (previously known as CRF2-4), belonging to the class II cytokine receptor family.
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPAPISSHC RLDKSNFQQP YITNRTFMLA KEASLADNNT DVRLIGEKLF HGVSMSERCY LMKQVLNFTL EEVLFPQSDR FQPYMQEVVP FLARLSNRLS TCHIEGDDLH IQRNVQKLKD TVKKLGESGE IKAIGELDLL FMSLRNACIH HHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Phosphoglycerate Kinase 1 Human Recombinant

Phosphoglycerate kinase 1, Primer recognition protein 2, Cell migration-inducing gene 10 protein, PRP 2, PGKA, MIG10, MGC8947, MGC117307, MGC142128, PGK1.

Product # :

PKA-351

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Description

PGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 437 amino acids (1-417 a.a.) and having a molecular mass of 46.8kDa. PGK1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGK1 solution containing 20mM Tris (pH 8.0), 10% Glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PGK1 is an X-linked enzyme that has a major role in the glycolytic pathway. PGK1 is a glycolytic enzyme which catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate, generating an ATP molecule. PGK1 may also act as a cofactor for polymerase alpha. Defects in the PGK1 gene are usually associated with chronic hemolytic anemia, though it can be accompanied by either mental retardation or muscular disease (rhabdomyolysis). Overexpression of PGK1 and its signalling targets are possibly an expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination. It was shown that PGK1 is differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
Synonyms
Phosphoglycerate kinase 1, Primer recognition protein 2, Cell migration-inducing gene 10 protein, PRP 2, PGKA, MIG10, MGC8947, MGC117307, MGC142128, PGK1.
Physical Appearance
Sterile filtered colorless solution.
Stability
PGK1 although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

SPARC Like 1 Mouse Recombinant

Sparcl1, Ecm2, hevin, mast9, Sc1, SPARC-like protein 1, Extracellular matrix protein 2, Matrix glycoprotein Sc1.

Product # :

PRO-2617

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Description

SPARCL1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 642 amino acids (17-650 a.a) and having a molecular mass of 71.7kDa.SPARCL1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SPARCL1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SPARC-like protein 1 or SPARC1 is an anti-adhesive protein with a similarity to the SPARC protein’s structure. SPARC1 is highly expressed in several tissues such as brain, lungs, kidney, heart, although it is not found in the liver tissue. The protein inhibits spreading or adhesion of many substrates and is considered to lead to antiadhesive signaling that stops neuronal migration, that occurs during development or as a trauma response, consistent with production by glial and neuronal cells.
Synonyms
Sparcl1, Ecm2, hevin, mast9, Sc1, SPARC-like protein 1, Extracellular matrix protein 2, Matrix glycoprotein Sc1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
IPTSTRFLSD HSNPTTATLV TPEDATVPIA GVEATADIEN HPSDKAEKPS ALNSEEETHE
QSTEQDKTYS FEVDLKDEED GDGDLSVDPT EGTLTLDLQE GTSEPQQKSL PENGDFPATV
STSYVDPNQR ANITKGKESQ EQPVSDSHQQ PNESSKQTQD LKAEESQTQD PDIPNEEEEE
EEDEEEEEEE EPEDIGAPSD NQEEGKEPLE EQPTSKWEGN REQSDDTLEE SSQPTQISKT
EKHQSEQGNQ GQESDSEAEG EDKAAGSKEH IPHTEQQDQE GKAGLEAIGN QKDTDEKAVS
TEPTDAAVVP RSHGGAGDNG GGDDSKHGAG DDYFIPSQEF LEAERMHSLS YYLKYGGGEE
TTTGESENRR EAADNQEAKK AESSPNAEPS DEGNSREHSA GSCTNFQCKR GHICKTDPQG
KPHCVCQDPE TCPPAKILDQ ACGTDNQTYA SSCHLFATKC RLEGTKKGHQ LQLDYFGACK
SIPACTDFEV AQFPLRMRDW LKNILMQLYE PNPKHGGYLN EKQRSKVKKI YLDEKRLLAG
HPIELLLRD FKKNYHMYVY PVHWQFNELD QHPADRILTH SELAPLRASL VPMEHCITRF
FEECDPNKDK HITLKEWGHC FGIKEEDIDE NLLFLEHHHH HH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Signal-Regulatory Protein Gamma Human Recombinant, Sf9

Signal Regulatory Protein Gamma, CD172 Antigen-Like Family Member B, Signal-Regulatory Protein Beta-2, Signal-Regulatory Protein Gamma, CD172g Antigen, SIRP-Gamma, SIRP-B2, SIRPB2, Signal-Regulatory Protein Beta 2, SIRP-Beta-2, SIRP Beta 2, SIRPgamma, BA77C3.1, CD172g.

Product # :

PRO-2435

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Description

SIRPG Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 574 amino acids (29-360a.a.) and having a molecular mass of 64.0kDa. SIRPG is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SIRPG protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 1 ug/ml and is measured by its binding ability in a functional ELISA with Human CD47.

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Introduction
Signal-Regulatory Protein Gamma (SIRPG) belongs to the signal-regulatory protein (SIRP) family whose members are receptor-type transmembrane glycoproteins which negatively regulate the receptor tyrosine kinase-coupled signaling processes. SIRPG is also a part of the immunoglobulin superfamily.
Synonyms
Signal Regulatory Protein Gamma, CD172 Antigen-Like Family Member B, Signal-Regulatory Protein Beta-2, Signal-Regulatory Protein Gamma, CD172g Antigen, SIRP-Gamma, SIRP-B2, SIRPB2, Signal-Regulatory Protein Beta 2, SIRP-Beta-2, SIRP Beta 2, SIRPgamma, BA77C3.1, CD172g.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPEEELQMI QPEKLLLVTV GKTATLHCTV TSLLPVGPVL WFRGVGPGRE LIYNQKEGHF PRVTTVSDLT KRNNMDFSIR ISSITPADVG TYYCVKFRKG SPENVEFKSG PGTEMALGAK PSAPVVLGPA ARTTPEHTVS FTCESHGFSP RDITLKWFKN GNELSDFQTN VDPTGQSVAY SIRSTARVVL DPWDVRSQVI CEVAHVTLQG DPLRGTANLS EAIRVPPTLE VTQQPMRVGN QVNVTCQVRK FYPQSLQLTW SENGNVCQRE TASTLTENKD GTYNWTSWFL VNISDQRDDV VLTCQVKHDG QLAVSKRLAL EVTVHQKDQS SDATPLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Selectin P Ligand Human Recombinant

Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.

Product # :

PRO-2714

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Description

SELPLG Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 496 amino acids (42-295 a.a) and having a molecular mass of 53.4kDa.SELPLG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The SELPLG solution (1mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SELPLG glycoprotein functions as a high affinity counter-receptor for the cell adhesion selectin molecules (P, E and L) located in stimulated T lymphocytes and myeloid cells. SELPLG binds leukocytes to activated platelets or endothelia expressing selectins, a vital role in leukocyte trafficking throughout inflammation. In order to have a high-affinity binding activity SELPLG needs two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. Polymorphisms and abnormal expression of SELPLG are linked to defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.
Synonyms
Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSQATEYEY LDYDFLPETE PPEMLRNSTD TTPLTGPGTP ESTTVEPAAR RSTGLDAGGA VTELTTELAN MGNLSTDSAA MEIQTTQPAA TEAQTTPLAA TEAQTTRLTA TEAQTTPLAA TEAQTTPPAA TEAQTTQPTG LEAQTTAPAA MEAQTTAPAA MEAQTTPPAA MEAQTTQTTA MEAQTTAPEA TEAQTTQPTA TEAQTTPLAA MEALSTEPSA TEALSMEPTT KRGLFIPFSV SSVTHKGIPM AASNLSVLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 1 Human Recombinant

Complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1, NDUFAF1, CIA30, CGI-65, CGI65.

Product # :

ENZ-661

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Description

NDUFAF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 326 amino acids (25-327) and having a molecular mass of 37kDa.NDUFAF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NDUFAF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4 (NDUFAF4) is involved in the compilation of mitochondrial NADH: ubiquinone oxidoreductase complex (complex I). In addition, NDUFAF4 is involved in cell proliferation and survival of hormone-dependent tumor cells. NDUFAF4 may also be a regulator of breast tumor cell invasion. NDUFAF4 gene mutations cause the mitochondrial complex I deficiency.
Synonyms
Complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1, NDUFAF1, CIA30, CGI-65, CGI65.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSYPFLGIR FAEYSSSLQK PVASPGKASS QRKTEGDLQG DHQKEVALDI TSSEEKPDVS FDKAIRDEAI YHFRLLKDEI VDHWRGPEGH PLHEVLLEQA KVVWQFRGKE DLDKWTVTSD KTIGGRSEVF LKMGKNNQSA LLYGTLSSEA PQDGESTRSG YCAMISRIPR GAFERKMSYD WSQFNTLYLR VRGDGRPWMV NIKEDTDFFQ RTNQMYSYFM FTRGGPYWQE VKIPFSKFFF SNRGRIRDVQ HELPLDKISS IGFTLADKVD GPFFLEIDFI GVFTDPAHTE EFAYENSPEL NPRLFK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cytokeratin 20 Human Recombinant

Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.

Product # :

PRO-351

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Description

Cytokeratin 20 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain having a molecular mass of 48,553 Dalton. The KRT20 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/1ml) was lyophilized after from a sterile solution containing 30mM Tris-HCL pH-8, 9.5M urea, 2mM DDT, 2mM EDTA and 10mM methylammonium chloride.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
KRT20 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21.
Synonyms
Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KRT20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT20 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized KRT20 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Reconstitution to filaments
Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5 M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4 M urea and then to low salt condition (50 mM NaCI, 2 mM dithiothreitol, 10 mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cleavage Stimulation Factor 1 Human Recombinant

Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

Product # :

PRO-1170

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Description

CSTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-431 a.a) and having a molecular mass of 49.4kDa.CSTF1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CSTF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.
Synonyms
Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DVEHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Uncoupling protein 3 Human Recombinant

Product # :

PRO-2821

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Description

The UCP3 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCP3 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 34 amino acid residues of the Resistin Human, 181-214 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized UCP3 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Uncoupling protein 3 (UCP3) is a mitochondrial protein which takes part in energy metabolism and thermoregulation.
UCP3 Function
Proton Uncoupling - UCP3 helps dissipate the proton gradient across the inner mitochondrial membrane. This uncoupling leads to the production of heat instead of ATP, a necessary process for thermogenesis.
Energy Regulation - UCP3 takes part in the regulation of energy expenditure and can influence metabolic efficiency.
UCP3 Location
UCP3 is predominantly expressed in skeletal muscle and brown adipose tissue, where its activity is critical for energy metabolism.
UCP3 Role in Metabolism
according to some studies, UCP3 may improve insulin sensitivity and help manage body weight. In addition, UCP3 participates in the metabolism of fatty acids and may help reduce the accumulation of reactive oxygen species (ROS) by decreasing oxidative stress.
UCP3 Regulation
UCP3 expression can raise in response to physical activity, emphasising its role in adapting to varius energy demands during exercise.
Changes in UCP3 levels have been associated with diabetes, obesity and other metabolic disorders.
Clinical Relevance
UCP3 is being investigated as a potential target for obesity and metabolic disease treatments because of its role in energy balance
UCP3 is a central player in energy metabolism and thermogenesis, with implications for metabolic health and the body's response to exercise and diet.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor Receptor, CHO Human Recombinant

Epidermal Growth Factor Receptor, Receptor Tyrosine-Protein Kinase ErbB-1, Erb-B2 Receptor Tyrosine Kinase, Proto-Oncogene C-ErbB-1, EC 2.7.10.1, ERBB1, ERBB, HER1, Epidermal Growth Factor Receptor (Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog), Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog (Avian), Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog, Cell Proliferation-Inducing Protein 61, Cell Growth Inhibiting Protein 40, EC 2.7.10, NISBD2, PIG61, MENA.

Product # :

PKA-086

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Description

EGFR produced in CHO cells is a single, glycosylated polypeptide chain containing 860 amino acids (25-645 a.a.) and having a molecular mass of 95.5 kDa (Migrates at 100-150 on SDS-PAGE under reducing conditions). EGFR is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary cells.

Formulation

EGFR protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGFa , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
Synonyms
Epidermal Growth Factor Receptor, Receptor Tyrosine-Protein Kinase ErbB-1, Erb-B2 Receptor Tyrosine Kinase, Proto-Oncogene C-ErbB-1, EC 2.7.10.1, ERBB1, ERBB, HER1, Epidermal Growth Factor Receptor (Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog), Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog (Avian), Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog, Cell Proliferation-Inducing Protein 61, Cell Growth Inhibiting Protein 40, EC 2.7.10, NISBD2, PIG61, MENA.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
LEEKKVCQGT SNKLTQLGTF EDHFLSLQRM FNNCEVVLGN LEITYVQRNY DLSFLKTIQE VAGYVLIALN TVERIPLENL QIIRGNMYYE NSYALAVLSN YDANKTGLKE LPMRNLQEIL HGAVRFSNNP ALCNVESIQW RDIVSSDFLS NMSMDFQNHL GSCQKCDPSC PNGSCWGAGE ENCQKLTKII CAQQCSGRCR GKSPSDCCHN QCAAGCTGPR ESDCLVCRKF RDEATCKDTC PPLMLYNPTT YQMDVNPEGK YSFGATCVKK CPRNYVVTDH GSCVRACGAD SYEMEEDGVR KCKKCEGPCR KVCNGIGIGE FKDSLSINAT NIKHFKNCTS ISGDLHILPV AFRGDSFTHT PPLDPQELDI LKTVKEITGF LLIQAWPENR TDLHAFENLE IIRGRTKQHG QFSLAVVSLN ITSLGLRSLK EISDGDVIIS GNKNLCYANT INWKKLFGTS GQKTKIISNR GENSCKATGQ VCHALCSPEG CWGPEPRDCV SCRNVSRGRE CVDKCNLLEG EPREFVENSE CIQCHPECLP QAMNITCTGR GPDNCIQCAH YIDGPHCVKT CPAGVMGENN TLVWKYADAG HVCHLCHPNC TYGCTGPGLE GCPTNGPKIP SRSPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Alcohol Dehydrogenase 1C, Human Recombinant, sf9

ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.

Product # :

ENZ-1010

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Description

ADH1C Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa. ADH1C is fused to a 6 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ADH1C protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

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Introduction
ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.
Synonyms
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF DLLRSGKSIR
TVLTFHHHHH H.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor Mouse Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-326

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Quantity :

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Description

Epidermal Growth Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids including 3 intramolecular disulfide-bonds and having a molecular mass of 6 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

More Info

Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.
Background
Exploring Novel Frontiers: Epidermal Growth Factor Mouse Recombinant and its Potential Therapeutic Implications
Abstract:
This research paper delves into the uncharted realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), unraveling its intricate molecular attributes, cellular signaling, and therapeutic prospects. Employing state-of-the-art methodologies involving genetic engineering, in vitro assays, and animal models, this study uncovers the multifaceted responses elicited by EGF-MR. The findings underscore its promise as a versatile therapeutic agent, potentially revolutionizing regenerative medicine and cancer interventions.
Introduction:
Epidermal Growth Factor (EGF) plays a pivotal role in cellular dynamics. This paper ventures into the nuanced landscape of Epidermal Growth Factor Mouse Recombinant (EGF-MR), delving into its unique molecular characteristics and exploring the therapeutic horizons it presents.
Molecular Insights and Receptor Binding:
EGF-MR's interaction with the epidermal growth factor receptor (EGFR) sets the stage for intricate intracellular events. High-resolution structural analyses and binding kinetics studies elucidate the nuances of this interaction, revealing structural motifs that initiate downstream signaling cascades.
Cellular Signaling and Functional Responses:
EGF-MR initiates canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K)/Akt pathways. Through comprehensive phosphoproteomic analyses and live-cell imaging, the spatiotemporal dynamics of EGF-MR-induced responses come to light, showcasing its role in cell proliferation, migration, and anti-apoptotic effects.
Genetic Engineering and In Vitro Assays:
Precise genetic manipulation ensures optimal EGF-MR expression. Gene codon optimization and signal peptide selection are meticulously undertaken to facilitate efficient protein synthesis and secretion. In vitro assays, encompassing cell viability and wound healing studies, illuminate EGF-MR's impact on cellular behaviors.
In Vivo Implications and Therapeutic Prospects:
In animal models, EGF-MR emerges as a transformative factor in tissue regeneration. Customized wound healing assays unveil its potential in accelerating re-epithelialization and granulation tissue formation. Moreover, the modulation of tumor microenvironments suggests its applicability in cancer interventions.
Future Directions and Challenges:
While promising, challenges lie ahead, including understanding intricate cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosing regimens to harness EGF-MR's full therapeutic potential.
Conclusion:
In a convergence of advanced methodologies and visionary therapeutic possibilities, Epidermal Growth Factor Mouse Recombinant takes center stage. Its distinctive molecular interactions and diverse cellular orchestration offer a glimpse into the future of regenerative medicine and targeted cancer therapies, propelling scientific progress into uncharted territories.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6 kDa.

What is the source or expression system of EGF Protein?
Escherichia Coli.

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

What is the amino acid sequence of EGF Protein?
NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Uteroglobin Mouse Recombinant

Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

Product # :

CYT-746

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Description

Uteroglobin Mouse Recombinant produced in E.coli is a non-glycosylated disulfide-linked homodimeric protein containing 2x75 amino acids chains and having a molecular mass of 16.7kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Uteroglobin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.

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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
Synonyms
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized SCGB1A1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DICPGFLQVL EALLMESESG YVASLKPFNP GSDLQNAGTQ LKRLVDTLPQ ETRINIMKLT EKILTSPLCK QDLRF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage Inflammatory Protein-4 Human Recombinant (CCL18)

Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

Product # :

CHM-322

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Description

Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MIP-4 protein is lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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Introduction
Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.
Synonyms
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized MIP-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
Background
What is the molecular weight/Mw of CCL18 HUMAN Protein?
CCL18 HUMAN Protein has a total Mw of 7.8kDa.

What is the source or expression system of CCL18 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL18 HUMAN Protein?
CCL18 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL18 HUMAN Protein?
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CCL18 HUMAN Protein?
The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.

What applications can CCL18 HUMAN Protein be used in?
CCL18 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL18 HUMAN Protein?
The endotoxin level is minimal, CCL18 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL18 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL18 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin 9 Human Recombinant, Sf9, Active

Interleukin 9, Protein Il9, Il9, HP40, Cytokine P40, T-cell growth factor P40

Product # :

CYT-1143

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Description

IL-9 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 132 amino acids (19-144 aa) and having a molecular mass of 14.9kDa.IL-9 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL-9 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

Determined by cell proliferation assay using MO7e human megakaryocytic leukemic cells. ED50 range for this effect is ≤ 0.3 ng/ml.

SDS-PAGE

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Introduction
Interleukin-9 is a protein that acts as one of the regulators of hematopoiesis. IL-9 is an enhancer of cells and megakaryoblastic leukemic cells’ growth. Among this protein’s producers we can find cells like mast cells, Treg, NKT cells, Th17, Th2, ILC2, and Th9 cells in various amounts. Th9 are the primary CD4 cells (T cells) that IL-9 is produced in.
Synonyms
Interleukin 9, Protein Il9, Il9, HP40, Cytokine P40, T-cell growth factor P40
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN
TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKIHHHH HH
Background
What is the molecular weight/Mw of IL9 HUMAN, SF9 ACTIVE Protein?
IL9 HUMAN, SF9 ACTIVE Protein has a total Mw of 14.9kDa.

What is the source or expression system of IL9 HUMAN, SF9 ACTIVE Protein?
Sf9, Baculovirus cells.

What is the Purity of IL9 HUMAN, SF9 ACTIVE Protein?
IL9 HUMAN, SF9 ACTIVE Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL9 HUMAN, SF9 ACTIVE Protein?
Determined by cell proliferation assay using MO7e human megakaryocytic leukemic cells. ED50 range for this effect is ≤ 0.3 ng/ml.

What is the amino acid sequence of IL9 HUMAN, SF9 ACTIVE Protein?
QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN
TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKIHHHH HH.

What applications can IL9 HUMAN, SF9 ACTIVE Protein be used in?
IL9 HUMAN, SF9 ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL9 HUMAN, SF9 ACTIVE Protein?
The endotoxin level is minimal, IL9 HUMAN, SF9 ACTIVE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL9 HUMAN, SF9 ACTIVE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL9 HUMAN, SF9 ACTIVE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Platelet-Derived Growth Factor AA Human Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

Product # :

CYT-341

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Description

Platelet-Derived Growth Factor AA Human Recombinant is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 125 amino acids and having a total molecular mass of 28511 Dalton. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized without any additives.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependent proliferation of murine 3T3 indicator cells is < 0.32ng/ml, corresponding to a Specific Activity of 3,125x10³units/mg.

More Info

Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF
have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Platelet-Derived Growth Factor AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Platelet-derived Growth Factor-AA in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SIEEAVPAVC KTRTVIYEIP RSQVDPTSAN FLIWPPCVEV KRCTGCCNTS SVKCQPSRVH HRSVKVAKVE YVRKKPKLKE VQVRLEEHLE CACATTSLNP DYREEDTGRP RESGKKRKRK RLKPT.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor (Leu-21) Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-466

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.The EGF 21-Leu is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

More Info

Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.
Background
Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications
Abstract:
This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications.
Introduction:
Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance.
Molecular Insights and Signaling Dynamics:
The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis.
Experimental Profiling and Cellular Responses:
In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Prospects:
Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions.
Future Challenges and Prospects:
While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21).
Conclusion:
In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.

What is the source or expression system of EGF Protein?
Escherichia Coli.

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.

What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

I-309 Human Recombinant (CCL1)

Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

Product # :

CHM-312

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Description

I-309 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8504 Dalton. The I-309 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CCL1 protein was lyophilized with no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

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Introduction
Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.
Synonyms
Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized I-309 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized I-309 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Ser-Met-Gln.
Background
What is the molecular weight/Mw of CCL1 HUMAN Protein?
CCL1 HUMAN Protein has a total Mw of 8.5kDa.

What is the source or expression system of CCL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL1 HUMAN Protein?
CCL1 HUMAN Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL1 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Ser-Met-Gln.

What applications can CCL1 HUMAN Protein be used in?
CCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL1 HUMAN Protein?
The endotoxin level is minimal, CCL1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL1 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL1 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Ribosomal Protein L35A Human Recombinant

Ribosomal Protein L35a, Cell Growth-Inhibiting Gene 33 Protein, 60S Ribosomal Protein L35a, DBA5, L35A.

Product # :

PRO-1703

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Description

RPL35A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.9kDa.RPL35A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RPL35A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Ribosomes, the organelles which catalyze protein synthesis, contain a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and nearly 80 structurally different proteins. RPL35A is a component of the 60S subunit of the ribosomal protein and a member of the L35AE family of ribosomal proteins. RPL35A is situated in the cytoplasm. The rat protein is known to bind to both initiator and elongator tRNAs, therefore, it is located at the P site, or P and A sites, of the ribosome. Though RPL35A was initially mapped to chromosome 18, it has been proven that it is located at 3q29-qter. Transcript variants utilizing alternative transcription initiation sites and alternative polyA signals exist. As is typical for genes encoding ribosomal proteins, there are several processed pseudogenes of this gene spread all over the genome.
Synonyms
Ribosomal Protein L35a, Cell Growth-Inhibiting Gene 33 Protein, 60S Ribosomal Protein L35a, DBA5, L35A.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSGRLWS KAIFAGYKRG LRNQREHTAL LKIEGVYARD ETEFYLGKRC AYVYKAKNNT VTPGGKPNKT RVIWGKVTRA HGNSGMVRAK FRSNLPAKAI GHRIRVMLYP SRI

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-3 Canine Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-722

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Description

Interleukin-3 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 14 kDa. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 1X PBS pH7.4.

Purity

Greater than 97.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RPFSTDLPKQ YFTMINEIME MLNKSPSPSE EPLDSNEKET LLEDTLLRPN LDVFLNASSK FHKNGLLIWN NLKEFLPLLP TPTPRGEPIS IMENNWGDFQ RKLKKYLEAL DNFLNFKNKP.
Background
What is the molecular weight/Mw of IL 3 DOG Protein?
IL 3 DOG Protein has a total Mw of 14kDa.

What is the source or expression system of IL 3 DOG Protein?
Escherichia Coli.

What is the Purity of IL 3 DOG Protein?
IL 3 DOG Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 DOG Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

What is the amino acid sequence of IL 3 DOG Protein?
RPFSTDLPKQ YFTMINEIME MLNKSPSPSE EPLDSNEKET LLEDTLLRPN LDVFLNASSK FHKNGLLIWN NLKEFLPLLP TPTPRGEPIS IMENNWGDFQ RKLKKYLEAL DNFLNFKNKP.

What applications can IL 3 DOG Protein be used in?
IL 3 DOG Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 3 DOG Protein?
The endotoxin level is minimal, IL 3 DOG Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 3 DOG that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 3 DOG?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Ectonucleoside Triphosphate Diphosphohydrolase 6 Recombinant

ectonucleoside triphosphate diphosphohydrolase 6 isoform 1, CD39L2, dJ738P15.3, IL-6SAG, IL6ST2, NTPDase-6.

Product # :

PRO-2629

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Description

ENTPD6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447amino acids (61-484a.a.) and having a molecular mass of 48.7kDa. ENTPD6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ENTPD6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 6 or ENTPD6 is an enzyme, akin to E-type nucleotidases. E-type nucleotidases, for instance CD39, are responsible for extracellular nucleotides catabolism. ENTPD6 has four apyrase-conserved areas like all to E-type nucleotidases. Rather spliced transcript agents that codes various isoforms were discovered for the DNA segment.
Synonyms
ectonucleoside triphosphate diphosphohydrolase 6 isoform 1, CD39L2, dJ738P15.3, IL-6SAG, IL6ST2, NTPDase-6.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKWHRATA TQAFFSITRA APGARWGQQA HSPLGTAADG HEVFYGIMFD AGSTGTRVHV FQFTRPPRET PTLTHETFKA LKPGLSAYAD DVEKSAQGIR ELLDVAKQDI PFDFWKATPL VLKATAGLRL LPGEKAQKLL QKVKEVFKAS PFLVGDDCVS IMNGTDEGVS AWITINFLTG SLKTPGGSSV GMLDLGGGST QIAFLPRVEG TLQASPPGYL TALRMFNRTY KLYSYSYLGL GLMSARLAIL GGVEGQPAKD GKELVSPCLS PSFKGEWEHA EVTYRVSGQK AAASLHELCA ARVSEVLQNR VHRTEEVKHV DFYAFSYYYD LAAGVGLIDA EKGGSLVVGD FEIAAKYVCR TLETQPQSSP FSCMDLTYVS LLLQEFGFPR SKVLKLTRKI DNVETSWALG AIFHYIDSLN RQKSPAS

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

EMG1 Nucleolar Protein Human Recombinant

EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.

Product # :

PRO-1122

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Description

EMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 267 amino acids (1-244) and having a molecular mass of 29.1kDa.EMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EMG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
EMG1 is a 244 aa protein which has a role in ribosome biogenesis. EMG1 is a key protein in the small ribosomal subunit assembly, controls methylation during ribosome synthesis and takes part in pre-18S rRNA processing. EMG1 is localized to the nucleolus and a mutation in this gene is linked with Bowen-Conradi syndrome.
Synonyms
EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAPSDG FKPRERSGGE QAQDWDALPP KRPRLGAGNK IGGRRLIVVL EGASLETVKV GKTYELLNCD KHKSILLKNG RDPGEARPDI THQSLLMLMD SPLNRAGLLQ VYIHTQKNVL IEVNPQTRIP RTFDRFCGLM VQLLHKLSVR AADGPQKLLK VIKNPVSDHF PVGCMKVGTS FSIPVVSDVR ELVPSSDPIV FVVGAFAHGK VSVEYTEKMV SISNYPLSAA LTCAKLTTAF EEVWGVI

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

RAB3B, Member RAS Oncogene Family Human Recombinant

RAB3B member RAS oncogene family, brain antigen RAB3B, ras-related protein Rab-3B.

Product # :

PRO-875

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Description

RAB3B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (1-219) and having a molecular mass of 26.9 kDa.The RAB3B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RAB3B protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 2mM DTT and 20% Glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
RAB3B which belongs to the RAS oncogene family is an extremely homologous monomeric GTPase that takes part in endocytosis and biosynthetic protein transport. The transport of recently synthesized proteins from the endoplasmic reticulum to several stacks of the Golgi complex and to secretory vesicles includes in every phase the movement of carrier vesicles.
Synonyms
RAB3B member RAS oncogene family, brain antigen RAB3B, ras-related protein Rab-3B.
Physical Appearance
RAB3B is supplied as a sterile filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASVTDGKTG VKDASDQNFD YMFKLLIIGN SSVGKTSFLF RYADDTFTPA FVSTVGIDFK VKTVYRHEKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWATQI KTYSWDNAQV ILVGNKCDME EERVVPTEKG QLLAEQLGFD FFEASAKENI SVRQAFERLV DAICDKMSDS LDTDPSMLGS SKNTRLSDTP PLLQQNCSC.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CD8, Rat Anti-Mouse, Biotin

CD8, MAL, p32.

Product # :

ANT-281

Price :

Quantity :

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
CD8 is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. CD8 acts as a co-receptor, and the T-cell receptor on the T lymphocyte recognize antigen displayed by an antigen presenting cell (APC) in the context of class I MHC molecules. The functional CD8 is either a homodimer composed of two alpha chains, or a heterodimer composed of one alpha and one beta chain. Both alpha and beta chains share significant homology to immunoglobulin variable light chains.
CD8 identifies cytotoxic/suppressor t-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of t-cell mediated killing. CD8 alpha chains bind to class-I MHC molecules alpha-3 domains.
Synonyms
CD8, MAL, p32.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Purified Mouse LN T cells.
Ig Subclass
Rat IgM.
Clone
NYRmCD8.
Applications
FACS staining, immunohistochemistry, Western Blotting. For staining, use 10 µl/1,000,000 cells.
Available Conjugates
This antibody is only available unconjugated and conjugated to FITC.
Type
Rat Anti Mouse Monoclonal.
Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion Exchange Column.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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