Search: 1000 results found for "angiogenin"

Description:

Plasminogen Activator Inhibitor-2 Mouse Recombinant

Serpnie2, B230326M24Rik, PAI-1, PI-7, PI7, PN-1, Spi4, Glia-derived nexin, GDN,Peptidase inhibitor 7, Protease nexin 1, Protease nexin I, Serine protease-inhibitor 4, Serpin E2.

Product # :

ENZ-972

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Description

SERPINE2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 386 amino acids (20-397a.a.) and having a molecular mass of 42.9kDa. SERPINE2 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SERPINE2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Plasminogen Activator Inhibitor-2 (Serpine2) which inhibits thrombin, plasmin and plasminogen activators is a part of the Serpin superfamily of the serine protease inhibitors. Serpine2 is able to transform human embryonic kidney cells into neuron-like cells. Furthermore, Serpine2's over expression in mice leads to progressive neuronal and motor dysfunction.
Synonyms
Serpnie2, B230326M24Rik, PAI-1, PI-7, PI7, PN-1, Spi4, Glia-derived nexin, GDN,Peptidase inhibitor 7, Protease nexin 1, Protease nexin I, Serine protease-inhibitor 4, Serpin E2.
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
SQFNSLSLEE LGSNTGIQVF NQIIKSRPHE NVVVSPHGIA SILGMLQLGA DGKTKKQLST VMRYNVNGVG KVLKKINKAI VSKKNKDIVT VANAVFLRNG FKMEVPFAVR NKDVFQCEVQ NVNFQDPASA SESINFWVKN ETRGMIDNLL SPNLIDGALT RLVLVNAVYF KGLWKSRFQP ESTKKRTFVA GDGKSYQVPM LAQLSVFRSG STRTPNGLWY NFIELPYHGE SISMLIALPT ESSTPLSAII PHITTKTIDS WMNTMVPKRM QLVLPKFTAV AQTDLKEPLK ALGITEMFEP SKANFTKITR SESLHVSHIL QKAKIEVSED GTKASAATTA ILIARSSPPW FIVDRPFLFS IRHNPTGAIL FLGQVNKPLE 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:

Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1 Mouse Recombinant, Sf9

Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, LYVE-1, Cell surface retention sequence-binding protein 1, CRSBP-1, Hyaluronic acid receptor, Extracellular link domain-containing protein.

Product # :

PKA-251

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Description

Soluble LYVE1 Mouse Recombinant fused to a C-terminal His-tag (6xHis) produced in baculovirus is a monomeric, glycosylated, polypeptide containing 228 amino acids (Met-1 to Gly 228) and having a molecular mass of 25 kDa but as a result of glycosilation the Mw is 40 kDa. The LYVE-1 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

LYVE1 was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

Greater than 95.0% as determined by:
(a)Analysis by RP-HPLC.
(b)Analysis by SDS-PAGE.

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Introduction
LYVE-1 has been identified as a major receptor for HA (extracellular matrix glycosaminoglycan hyaluronan) on the lymph vessel wall. The deduced amino acid sequence of LYVE-1 predicts a 322-residue type I integral membrane polypeptide 41% similar to the CD44 HA receptor with a 212-residue extracellular domain containing a single Link module the prototypic HA binding domain of the Link protein superfamily. Like CD44, the LYVE-1 molecule binds both soluble and immobilized HA. However, unlike CD44, the LYVE-1 molecule colocalizes with HA on the luminal face of the lymph vessel wall and is completely absent from blood vessels. Hence, LYVE-1 is the first lymph-specific HA receptor to be characterized and is a uniquely powerful marker for lymph vessels themselves.
Synonyms
Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, LYVE-1, Cell surface retention sequence-binding protein 1, CRSBP-1, Hyaluronic acid receptor, Extracellular link domain-containing protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized sLYVE-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sLYVE-1 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 LYVE1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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:

Osteopontin Human Recombinant

Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

Product # :

CYT-635

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Description

Secreted Phosphoprotein-1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 321 amino acids fragment (17-314) and having a total molecular mass of 36.2 kDa(molecular weight on SDS-PAGE will shift up). The SPP1 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Osteopontin is supplied in 20mM Tris-HCl buffer pH-7.5, 1mM DTT, 2mM EDTA and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.
Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
Physical Appearance
Sterile Filtered clear 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 RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV N.

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:

Desert Hedgehog (C23II) Mouse Recombinant

Desert hedgehog protein, DHH, HHG-3, C78960.

Product # :

CYT-773

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Description

DHH (C23II) Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 20kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4, 1mM DTT and 0.05% Tween-80.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to induce alkaline phosphatase production by murine MC3T3-E1 cells is 5-20 µg/ml.

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Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.
Synonyms
Desert hedgehog protein, DHH, HHG-3, C78960.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IIGPGRGPVG RRRYVRKQLV PLLYKQFVPS MPERTLGASG PAEGRVTRGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH IHVSVKADNS LAVRAGG.

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:

Fibroblast Growth Factor-8 Mouse Recombinant, 194 a.a.

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Product # :

CYT-840

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Description

FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 5mM Na3PO4 and 50 mM NaCl, pH 7.5.

Purity

Greater than 97.0% as determined by analysis by SDS-PAGE.

Biological Activity

The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

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Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF 8 although stable at room temperature for 3 weeks, should be stored desiccated below -18?C. Upon reconstitution FGF 8 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 FGF 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 22.5kDa.

What is the source or expression system of FGF8 Protein?
Escherichia Coli.

What is the Purity of FGF8 Protein?
FGF8 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF8 Protein?
The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

What is the amino acid sequence of FGF8 Protein?
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 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:

Fibroblast Growth Factor-6 Human Recombinant

Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.

Product # :

CYT-979

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Description

FGF6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 169 amino acids and having a molecular mass of 18.9kDa.The FGF-6 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-6 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 50mM sodium chloride pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Fibroblast Growth Factor-6 (FGF6) belongs to the fibroblast growth factor (FGF) family. FGF family members possess extensive mitogenic and cell survival functions, and are involved in various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF6 gene displayes oncogenic transforming activity when transfected into mammalian cells. The mouse homolog of the FGF6 gene displays a restricted expression profile predominantly in the myogenic lineage, suggesting a role in muscle regeneration or differentiation.
Synonyms
Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-6 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 FGF6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.
Background
What is the molecular weight/Mw of FGF6 Protein?
FGF6 Protein has a total Mw of 18.9kDa.

What is the source or expression system of FGF6 Protein?
Escherichia Coli.

What is the Purity of FGF6 Protein?
FGF6 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF6 Protein?
The biological functionality of FGF6 Protein will be determined in the future.

What is the amino acid sequence of FGF6 Protein?
MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.

What applications can FGF6 Protein be used in?
FGF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF6 Protein?
The endotoxin level is minimal, FGF6 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:

Retinoblastoma Associated Protein Human Recombinant

RB, OSRC, RB-1, RB1, p105-Rb, OSTEOSARCOMA, RETINOBLASTOMA-RELATED,PP110, Retinoblastoma-associated protein.

Product # :

PRO-584

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Description

Retinoblastoma Human Recombinant fused with 6X His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.5 kDa.The Retinoblastoma is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RB1 was lyophilized from 1xPBS pH-7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Retinoblastoma (RB) is an embryonic malignant neoplasm of retinal origin. It almost always presents in early childhood and is often bilateral. Spontaneous regression ('cure') occurs in some cases. Retinoblastoma acts as a regulator of other genes and forms a complex with adenovirus e1a and with sv40 large t antigen. Retinoblastoma acts as a tumor suppressor and modulats functionally certain cellular proteins with which t and e1a compete for pocket binding. Retinoblastoma is potent inhibitor of e2f-mediated trans-activation, recruits and targets histone methyltransferase suv39h1 leading to epigenetic transcriptional repression, inhibits the intrinsic kinase activity of taf1.
Synonyms
RB, OSRC, RB-1, RB1, p105-Rb, OSTEOSARCOMA, RETINOBLASTOMA-RELATED,PP110, Retinoblastoma-associated protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Retinoblastoma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Retinoblastoma 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 Retinoblastoma in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MASFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFG
TSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSK
HLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEKHHHHHH.

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:

Stress-Induced Protein SAM22 Recombinant

Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

Product # :

PRO-2278

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Description

Recombinant Stress-Induced Protein SAM22 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 19,484 Dalton. Gly m 4.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

Gly m 4.0101 is supplied in in 20mM HEPES buffer pH-7.9 and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.
Synonyms
Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

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:

Tick-Borne Encephalitis Virus Core Protein Recombinant

Product # :

TBE-285

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Description

The E.coli derived recombinant protein contains the Tick-borne Encephalitis Virus core protein epitopes.

Source

Escherichia Coli.

Formulation

20mM MES pH 6.5, 8M urea, 200mM NaCl & 0.05% Tween-20.

Purity

Encephalitis protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
TBE is caused by tick-borne encephalitis virus (TBEV), a member of the family Flaviviridae.
A closely related virus in Far Eastern Eurasia, Russian spring-summer encephalitis virus (RSSEV).
The family Flaviviridae includes other tick-borne viruses are closely related to TBEV and RSSEV, such as Omsk hemorrhagic fever virus & Kyasanur Forest virus.
Louping ill virus is also a member of this family.
Stability
Encephalitis protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
Encephalitis antigen is suitable for ELISA and Western blots, excellent antigen for detection of Tick-borne encephalitis virus with minimal specificity problems.
Specificity
Immunoreactive with sera of encephalitis virus infected individuals.
Purification Method
Encephalitis protein was purified by proprietary chromatographic technique.

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:

Monocyte Chemotactic Protein-2 Canine Recombinant (CCL8)

C-C motif chemokine 8, Monocyte chemoattractant protein 2, Monocyte chemotactic protein 2, MCP-2, Small-inducible cytokine A8, CCL8, MCP2.

Product # :

CHM-285

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Quantity :

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Description

MCP2 Canine Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.8kDa.The CCL8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MCP-2 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

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

Biological Activity

The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 10-100 ng/ml.

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Introduction
Chemokine (C-C motif) ligand 8 (CCL8) is a small cytokine belonging to the CC chemokine family that was once called monocyte chemotactic protein-2 (MCP-2). The CCL8 protein is produced as a precursor containing 109 amino acids, which is cleaved to produce mature CCL8 containing 75 amino acids. The gene for CCL8 is encoded by 3 exons and is located within a large cluster of CC chemokines on chromosome 17q11.2 in humans. MCP-2 is chemotactic for and activates a many different immune cells, including mast cells, eosinophils and basophils, (that are implicated in allergic responses), and monocytes, T cells, and NK cells that are involved in the inflammatory response. CCL8 elicits its effects by binding to several different cell surface receptors called chemokine receptors. These receptors include CCR1, CCR2B and CCR5.
Synonyms
C-C motif chemokine 8, Monocyte chemoattractant protein 2, Monocyte chemotactic protein 2, MCP-2, Small-inducible cytokine A8, CCL8, MCP2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL8 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 MCP2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDSVSIPIT CCFSMVKRKI PMQKLESYMR ITNSQCPQEA VIFKTKASRE ICADPKQKWV QDYMNHLDQK SQAQKP.
Background
What is the molecular weight/Mw of CCL8 CANINE Protein?
CCL8 CANINE Protein has a total Mw of 8.8kDa.

What is the source or expression system of CCL8 CANINE Protein?
Escherichia Coli.

What is the Purity of CCL8 CANINE Protein?
CCL8 CANINE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL8 CANINE Protein?
The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 10-100 ng/ml.

What is the amino acid sequence of CCL8 CANINE Protein?
QPDSVSIPIT CCFSMVKRKI PMQKLESYMR ITNSQCPQEA VIFKTKASRE ICADPKQKWV QDYMNHLDQK SQAQKP.

What applications can CCL8 CANINE Protein be used in?
CCL8 CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL8 CANINE Protein?
The endotoxin level is minimal, CCL8 CANINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL8 CANINE 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 CCL8 CANINE?
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:

Polypeptide N-Acetylgalactosaminyltransferase 1 Human Recombinant

Polypeptide N-acetylgalactosaminyltransferase 1, GALNT1, GALNAC-T1

Product # :

enz-1098

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Description

GALNT1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 528 amino acids (41-559a.a.) and having a molecular mass of 60.4kDa.GALNT1 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

GALNT1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) containing 0.1M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The specific activity which is defined as the amount of enzyme that transfer 1.0 pmole of GalNAc from UDP-GalNAc to peptide EA2 per minute at pH 8.0 at 37C is > 300 pmol/min/ug.

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Introduction
Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) is a part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.
Synonyms
Polypeptide N-acetylgalactosaminyltransferase 1, GALNT1, GALNAC-T1
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
ADPGLPAGDV LEPVQKPHEG PGEMGKPVVI PKEDQEKMKE MFKINQFNLM ASEMIALNRS
LPDVRLEGCK TKVYPDNLPT TSVVIVFHNE AWSTLLRTVH SVINRSPRHM IEEIVLVDDA
SERDFLKRPL ESYVKKLKVP VHVIRMEQRS GLIRARLKGA AVSKGQVITF LDAHCECTVG
WLEPLLARIK HDRRTVVCPI IDVISDDTFE YMAGSDMTYG GFNWKLNFRW YPVPQREMDR
RKGDRTLPVR TPTMAGGLFS IDRDYFQEIG TYDAGMDIWG GENLEISFRI WQCGGTLEIV
TCSHVGHVFR KATPYTFPGG TGQIINKNNR RLAEVWMDEF KNFFYIISPG VTKVDYGDIS
SRVGLRHKLQ CKPFSWYLEN IYPDSQIPRH YFSLGEIRNV ETNQCLDNMA RKENEKVGIF
NCHGMGGNQV FSYTANKEIR TDDLCLDVSK LNGPVTMLKC HHLKGNQLWE YDPVKLTLQH
VNSNQCLDKA TEEDSQVPSI RDCNGSRSQQ WLLRNVTLPE IFHHHHHH.

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:

Serum Amyloid A (APO-SAA) Feline Recombinant

Product # :

CYT-1221

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Description

SAA Feline produced in E.coli is a single, non-glycosylated polypeptide chain (1-111 a.a) containing 121 a.a and having a molecular mass of 13,838 Dalton. SAA s fused with a 10 amino acids His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SAA was lyophilized from 0.01M HCl (pH 2.0).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) 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 SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
In response to infection, injury, or inflammation, SAA levels rapidly rise in the bloodstream. Acting as a chemoattractant, SAA recruits immune cells to the site of injury, facilitating the innate immune response. Additionally, SAA modulates the activities of immune cells, influencing cytokine production and phagocytosis. These immunomodulatory functions highlight SAA's significance in shaping the immune landscape during inflammatory events. SAA participates in lipid metabolism by interacting with HDL particles. In the acute-phase response, SAA displaces apolipoprotein A1 from HDL, transforming it into a pro-inflammatory particle. This alteration in HDL composition affects its cardioprotective functions, potentially contributing to atherosclerosis and cardiovascular diseases. Understanding these interactions is crucial for deciphering the intricate relationship between inflammation and cardiovascular health.

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:

Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO

BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.

Product # :

CYT-1094

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Description

Bone Morphogenetic Protein Receptor-1A Human Recombinant produced in CHO cells is a glycosylated homodimer chain containing 2x362 amino acids and having a total molecular mass of 80.8kDa. BMPR1A is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg.

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Introduction
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
Synonyms
BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMPR1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMPR1A 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 BMPR1A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.
Background
Research Paper on Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer, HEK
Abstract:
Welcome to the captivating world of Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer (BMPR-1A HR) in Human Embryonic Kidney Cells (HEK). This research paper explores the vital role of BMPR-1A HR in cellular responses. As a key receptor in the transforming growth factor-beta (TGF-β) superfamily, BMPR-1A HR plays a significant part in guiding cellular differentiation and tissue development. Join us as we unravel the molecular mechanisms behind BMPR-1A HR signaling in HEK cells and delve into its interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the intriguing world of BMPR-1A HR! In this section, we introduce the remarkable BMPR-1A HR and its crucial role in shaping cellular responses. Together, let's explore how this receptor influences cellular behavior and contributes to tissue growth, fostering our understanding of its importance in biological processes.
BMPR-1A HR Signaling in HEK Cells:
Be amazed by the intricate dance of BMPR-1A HR signaling within HEK cells! Uncover the complex process of ligand-receptor binding, initiating both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay regulates a wide range of cellular processes, including gene transcription, cell proliferation, and differentiation, forming the foundation of cellular communication.
Influential Role in Cellular Responses:
Marvel at the influential role of BMPR-1A HR as a critical mediator of cellular responses within HEK cells. Witness its ability to modulate cellular differentiation, driving the expression of key differentiation markers such as DIF. Our exploration will highlight the multifaceted nature of BMPR-1A HR, impacting diverse cellular pathways, including those involving TNF-α and TNFSF2, shaping a dynamic and interconnected cellular network.
Interplay with Key Cytokines:
Discover the intriguing interactions between BMPR-1A HR and key cytokines like TNF-α and TNFSF2. Explore how BMPR-1A HR influences their expression and activity, hinting at potential cross-talk between BMPR-1A HR and inflammatory pathways. This delicate balance fosters a harmonious cellular environment, where multiple players contribute to overall cellular responses.
Therapeutic Implications and Tissue Development:
Witness the potential therapeutic implications of BMPR-1A HR in tissue development. Together, we explore the exciting possibilities of utilizing BMPR-1A HR in regenerative medicine, offering hope for enhanced tissue development and repair. As we venture forth, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring a responsible and effective approach.
Conclusion:
As we conclude our exploration of BMPR-1A HR in HEK cells, we stand in awe of its role in mediating cellular responses and tissue development. Equipped with this knowledge, we look forward to a promising future, where BMPR-1A HR from CHO cells opens doors to innovative applications in regenerative medicine, contributing to improved human health and well-being.
What is the molecular weight/Mw of BMPR1A Protein?
BMPR1A Protein has a total Mw of 80.8kDa.

What is the source or expression system of BMPR1A Protein?
CHO cells.

What is the Purity of BMPR1A Protein?
BMPR1A Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMPR1A Protein?
The ED50, as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg.

What is the amino acid sequence of BMPR1A Protein?
QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.

What applications can BMPR1A Protein be used in?
BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMPR1A Protein?
The endotoxin level is minimal, BMPR1A 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:

Stanniocalcin-2 Human Recombinant

Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

Product # :

HOR-296

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Description

Stanniocalcin-2 Human Recombinant produced in HEK 293 cell line is a single, glycosylated, polypeptide chain containing 289 amino acids and having a total molecular mass of 31.9kDa (calculated). The Stanniocalcin contains four extra residues which were used as a spacer and 8 residues form the C-Terminal Flag- tag.Stanniocalcin is purified by proprietary chromatographic techniques.The amino acid sequence of the recombinant human Stanniocalcin-2 is 100% homologous to the amino acid sequence AA 25-302 of the human mature Human Stanniocalcin-2.

Source

HEK 293 cell line (Human embryonic kidney).

Formulation

Filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris buffer, 20mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
STC2 is a homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive over expression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.
Synonyms
Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized STC-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Stanniocalcin 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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
TDATNPPEGP QDRSSQQKGR LSLQNTAEIQ HCLVNAGDVG CGVFECFENN SCEIRGLHGI CMTFLHNAGKFDAQGKSFIK DALKCKAHAL RHRFGCISRK CPAIREMVSQ LQRECYLKHD LCAAAQENTR VIVEMIHFKDLLLHEPYVDL VNLLLTCGEE VKEAITHSVQ VQCEQNWGSL CSILSFCTSA IQKPPTAPPE RQPQVDRTKLSRAHHGEAGH HLPEPSSRET GRGAKGERGS KSHPNAHARG RVGGLGAQGP SGSSEWEDEQ SEYSDIRRAAADYKDDDDK.

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:

MIG (CXCL9) Bovine Recombinant

Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.

Product # :

CHM-041

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Shipped at Room temp

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Description

MIG (CXCL9) BovineRecombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 104 amino acids and having a molecular mass of approximately 18.0kDa.MIG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.

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Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belongs to the CXC chemokine family that is also known as Monokine induced by gamma INF (MIG). CXCL9 is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
Synonyms
Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIG (CXCL9) 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 MIG (CXCL9) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPAIRNGRCS CINTSQGMIH PKSLKDLKQF APSPSCEKTE IIATMKNGNE ACLNPDLPEV KELIKEWEKQ VNQKKKQRKG KKYKKTKKVP KVKRSQRPSQ KKTT.
Background
What is the molecular weight/Mw of CXCL9 BOVINE Protein?
CXCL9 BOVINE Protein has a total Mw of 18kDa.

What is the source or expression system of CXCL9 BOVINE Protein?
Escherichia Coli.

What is the Purity of CXCL9 BOVINE Protein?
CXCL9 BOVINE Protein is > 96% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL9 BOVINE Protein?
The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.

What is the amino acid sequence of CXCL9 BOVINE Protein?
VPAIRNGRCS CINTSQGMIH PKSLKDLKQF APSPSCEKTE IIATMKNGNE ACLNPDLPEV KELIKEWEKQ VNQKKKQRKG KKYKKTKKVP KVKRSQRPSQ KKTT.

What applications can CXCL9 BOVINE Protein be used in?
CXCL9 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL9 BOVINE Protein?
The endotoxin level is minimal, CXCL9 BOVINE 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:

RANK Human Recombinant

TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265

Product # :

CYT-734

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Description

RANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.1kDa. The RANK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH 8.0 and 150mM NaCl.

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 its ability to inhibit sRANK Ligand induced nuclear factor kappa B (NFkappaB) in RAW 264.7 cells is less than 50 ng/ml, corresponding to a specific activity of
> 2.0 × 10⁴ IU/mg in the presence of 15 ng/ml of recombinant sRANK Ligand.

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Introduction
sRANK Receptor is a part of of the TNF superfamily of ligands and receptors which participates in the regulation of specific immunity and bone turnover. sRANK Receptor was originally acknowledged as a dendritic-cell-membrane protein, which by interacting with RANKL augments the capacity of dendritic cells to stimulate naive T cell proliferation and to endorse the survival of RANK and T cells. The full length human RANK cDNA encodes a type I transmembrane protein of 616 amino acids with a predicted 183 amino acid extracellular domain and a 383 amino acid cytoplasmic domain. sRANK Receptor is also expressed in a various tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.
Synonyms
TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized RANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANK Receptor 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 RANK in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QIAPPCTSEK HYEHLGRCCN KCEPGKYMSS KCTTTSDSVC LPCGPDEYLD SWNEEDKCLL HKVCDTGKAL VAVVAGNSTT PRRCACTAGY HWSQDCECCR RNTECAPGLG AQHPLQLNKD TVCKPCLAGY FSDAFSSTDK CRPWTNCTFL GKRVEHHGTE KSDAVCSSSL PARK.

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:

Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant, His Tag

14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

Product # :

PKA-262

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Shipped with Ice Packs

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Description

YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (2-247) and having a molecular mass of 36 kDa. YWHAG is fused to His Tag and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

YWHAG solution containing 1x PBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.
Synonyms
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.
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. Avoid multiple freeze-thaw cycles.

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-8 Canine Recombinant

Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8.

Product # :

CHM-009

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-8 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa. The IL8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected murine BaF3 cells is in a concentration range of 0.15-0.75 ng/ml.

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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL8 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 IL-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVLSRVSSEL RCQCIKTHST PFHPKYIKEL RVIDSGPHCE NSEIIVKLFN GNEVCLDPKE KWVQKVVQIF LKKAEKQDP.
Background
What is the molecular weight/Mw of CXCL8 CANINE Protein?
CXCL8 CANINE Protein has a total Mw of 9.1kDa.

What is the source or expression system of CXCL8 CANINE Protein?
Escherichia Coli.

What is the Purity of CXCL8 CANINE Protein?
CXCL8 CANINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 CANINE Protein?
The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected murine BaF3 cells is in a concentration range of 0.15-0.75 ng/ml.

What is the amino acid sequence of CXCL8 CANINE Protein?
AVLSRVSSEL RCQCIKTHST PFHPKYIKEL RVIDSGPHCE NSEIIVKLFN GNEVCLDPKE KWVQKVVQIF LKKAEKQDP.

What applications can CXCL8 CANINE Protein be used in?
CXCL8 CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 CANINE Protein?
The endotoxin level is minimal, CXCL8 CANINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 CANINE 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 CXCL8 CANINE?
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:

BPC-157 Pentadecapeptide

Product # :

HOR-029

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Description

BPC-157 Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BPC-157 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution bpc-157 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 BPC-157 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
Background
BPC-157, short for Body Protection Compound-157, is a synthetic peptide that has garnered significant attention in the field of regenerative medicine and sports science. This peptide, derived from a portion of the human gastric juice protein known as BPC, exhibits remarkable healing and tissue regeneration properties. BPC-157 has shown promise in various preclinical and clinical studies, demonstrating its potential for the treatment of a wide range of injuries and disorders.
The research on BPC-157 encompasses investigations into its mechanisms of action, efficacy, safety, and potential therapeutic applications. Studies have elucidated the peptide's ability to enhance angiogenesis, promote collagen synthesis, modulate inflammatory responses, and protect against oxidative stress. These properties make BPC-157 an intriguing candidate for accelerating tissue healing, reducing inflammation, and improving overall recovery outcomes.
Preclinical studies have revealed the beneficial effects of BPC-157 in several injury models. For instance, BPC-157 has demonstrated its potential in accelerating tendon and ligament healing, mitigating muscle damage, and promoting bone regeneration. These findings suggest that BPC-157 could be a valuable therapeutic tool in orthopedic medicine and sports-related injuries.
Furthermore, BPC-157 has exhibited promising effects on gastrointestinal health. Studies have highlighted its ability to protect and heal the gut lining, reduce ulcer formation, and alleviate symptoms associated with inflammatory bowel disease. These observations open up avenues for BPC-157 as a potential treatment for gastrointestinal disorders.
In addition to its regenerative properties, BPC-157 has shown potential in neurological and psychiatric conditions. Research has indicated its neuroprotective effects, with implications for the treatment of traumatic brain injury, stroke, and neurodegenerative disorders. Preliminary studies also suggest BPC-157's potential as an antidepressant and anxiolytic agent.
Despite the promising findings, further research is needed to fully understand the mechanisms underlying BPC-157's actions and to assess its long-term safety and efficacy. Clinical trials are underway to explore its potential therapeutic applications in humans, including its use in tendon and ligament repair, inflammatory bowel disease, and neurodegenerative disorders.
This comprehensive review aims to summarize the current state of research on BPC-157, providing an overview of its mechanisms of action and therapeutic potential. By examining relevant studies and findings, we aim to shed light on the diverse applications of BPC-157 and its implications for regenerative medicine, sports science, and various disease

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:

Galectin-14 Human Recombinant

Placental protein 13-like, Charcot-Leyden crystal protein 2, CLC2, Galectin-14, Gal-14, LGALS14, PPL13, MGC22235.

Product # :

CYT-003

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Description

LGALS14 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids (1-139 a.a.) and having a molecular mass of 18.5kDa. The LGALS14 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LGALS14 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Galectin14, aka LGALS14, is a member of the galectin family of carbohydrate binding proteins. Galectin family members contain one or two carbohydrate recognition domains, which can bind beta-galactoside. The LGALS14 gene is predominantly expressed in the placenta. LGALS14 is expressed intracellularly in the placenta and eosinophils and is released by eosinophils following allergen stimulation. LGALS14 may be involved in the development of allergic inflammation.
Synonyms
Placental protein 13-like, Charcot-Leyden crystal protein 2, CLC2, Galectin-14, Gal-14, LGALS14, PPL13, MGC22235.
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 MGSMSSLPVP YTLPVSLPVG SCVIITGTPI LTFVKDPQLE VNFYTGMDED SDIAFQFRLH FGHPAIMNSR VFGIWRYEEK CYYLPFEDGK PFELCIYVRH KEYKVMVNGQ RIYNFAHRFP PASVKMLQVL RDISLTRVLI SD.
Background
What is the molecular weight/Mw of LGALS14 HUMAN Protein?
LGALS14 HUMAN Protein has a total Mw of 18.5kDa.

What is the source or expression system of LGALS14 HUMAN Protein?
Escherichia Coli.

What is the Purity of LGALS14 HUMAN Protein?
LGALS14 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS14 HUMAN Protein?
The biological functionality of LGALS14 HUMAN Protein will be determined in the future.

What is the amino acid sequence of LGALS14 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSSLPVP YTLPVSLPVG SCVIITGTPI LTFVKDPQLE VNFYTGMDED SDIAFQFRLH FGHPAIMNSR VFGIWRYEEK CYYLPFEDGK PFELCIYVRH KEYKVMVNGQ RIYNFAHRFP PASVKMLQVL RDISLTRVLI SD.
What applications can LGALS14 HUMAN Protein be used in?
LGALS14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS14 HUMAN Protein?
The endotoxin level is minimal, LGALS14 HUMAN 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:

Leptin-B Tilapia Recombinant

Product # :

CYT-1110

Price :

Quantity :

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Shipped at Room temp

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Description

Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

Purity

Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin-B Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-B Tilapia 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 Leptin-B Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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:

Interferon-gamma Canine Recombinant

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-404

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Shipped at Room temp

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Description

Recombinant IFNG Dog produced in E.coli cells is a non-glycosylated, homodimeric protein containing 143 amino acid chain and having a molecular mass of 16.9kDa. IFNG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IFNG was lyophilized from a 0.2µm filtered concentrated solution in 25mM Sodium Succinate, pH 5.0, 60mM NaCl, with 0.1% Tween-80.

Purity

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

Biological Activity

The ED50 as determined by an anti-viral assay using A-72 canine fibroma cells infected with vesicular stomatitis virus (VSV) is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFNG 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 IFNG in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QAMFFKEIEN LKEYFNASNP DVSDGGSLFV DILKKWREES DKTIIQSQIV SFYLKLFDNF KDNQIIQRSM DTIKEDMLGK FLNSSTSKRE DFLKLIQIPV NDLQVQRKAI NELIKVMNDL SPRSNLRKRK RSQNLFRGRR ASK
Background
What is the molecular weight/Mw of IFNG CANINE Protein?
IFNG CANINE Protein has a total Mw of 16.9kDa.

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

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

What is the Biological Activity of IFNG CANINE Protein?
The ED50 as determined by an anti-viral assay using A-72 canine fibroma cells infected with vesicular stomatitis virus (VSV) is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

What is the amino acid sequence of IFNG CANINE Protein?
QAMFFKEIEN LKEYFNASNP DVSDGGSLFV DILKKWREES DKTIIQSQIV SFYLKLFDNF KDNQIIQRSM DTIKEDMLGK FLNSSTSKRE DFLKLIQIPV NDLQVQRKAI NELIKVMNDL SPRSNLRKRK RSQNLFRGRR ASK

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

What is the endotoxin level for IFNG CANINE Protein?
The endotoxin level is minimal, IFNG CANINE 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:

Cadherin-E Human Recombinant

Epithelial cadherin, E-cadherin, Uvomorulin, Cadherin-1, CAM 120/80, CD324 antigen, CDH1, CDHE, UVO, ECAD, LCAM, Arc-1, CD324, Cadherin-E.

Product # :

PRO-461

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Description

Cadherin-E Human Recombinant (aa 600-707) expressed in E.coli, shows a 38 kDa band on SDS-PAGE.The Cadherin-E is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Cadherin-E protein (100µg/1ml) in 50mM Tris-HCl, pH7.5 and 10mM L-glutathione (reduced).

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Introduction
E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.
Synonyms
Epithelial cadherin, E-cadherin, Uvomorulin, Cadherin-1, CAM 120/80, CD324 antigen, CDH1, CDHE, UVO, ECAD, LCAM, Arc-1, CD324, Cadherin-E.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
Amino Acid Sequence
iffcernpkpq viniidadlp pntspftael thgasanwti qyndptqesi ilkpkmalev gdykinlklm dnqnkdqvtt levsvcdceg aagvcrkaqp veaglqi.

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:

Matrix Metalloproteinase 12 (1-33 a.a.) Human Recombinant

Product # :

ENZ-1201

Price :

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Description

The MMP12 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MMP12 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 33 amino acid residues of the MMP12 Human, 1-33 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
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized MMP12 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.
Amino Acid Sequence
MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFG.
Background
Matrix Metalloproteinase 12 also known as MMP12 is 1 of the main enzymes in the MMP family which is primarily produced by macrophages and neutrophils. MMP12 is implicated in the breakdown of elastin and in the development of chronic inflammatory diseases, such as emphysema, COPD and atherosclerosis. MMP12 is upregulated and contributes to tissue remodeling in inflammatory responses which is essential for wound healing and immune defense. MMP12 catalyzes the cleavage of collagen, elastin and other ECM components. Its activity is regulated in normal tissues to avoid pathological degradation.

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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