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1000 results found for “gliadin”
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Name :
CHODL HumanDescription:
Chondrolectin Human Recombinant
Chondrolectin, Transmembrane Protein MT75, C21orf68, Chromosome 21 Open Reading Frame 68, PRED12, MT75, CHODL.
Product # :
PRO-1964Price :
Quantity :
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Shipped with Ice Packs
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Description
CHODL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (22-216) and having a molecular mass of 24.6 kDa.CHODL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHODL solution (1mg/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.
More Info
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Introduction
Chondrolectin (CHODL) is a type I membrane protein with a carbohydrate recognition domain characteristic of C-type lectins in its extracellular portion. In other proteins, this domain is involved in endocytosis of glycoproteins and exogenous sugar-bearing pathogens. The CHODL protein localizes mainly to the perinuclear region.
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Synonyms
Chondrolectin, Transmembrane Protein MT75, C21orf68, Chromosome 21 Open Reading Frame 68, PRED12, MT75, CHODL.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFCRRVVS GQKVCFADFK HPCYKMAYFH ELSSRVSFQE ARLACESEGG VLLSLENEAE QKLIESMLQN LTKPGTGISD GDFWIGLWRN GDGQTSGACP DLYQWSDGSN SQYRNWYTDE PSCGSEKCVV MYHQPTANPG LGGPYLYQWN DDRCNMKHNY ICKYEPEINP TAPVEKPYLT NQPGDTHQNV VVTEAGIIPN.
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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Name :
GroEL E.ColiDescription:
GroEL (HSP60) E.Coli Recombinant
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.
Product # :
HSP-004Price :
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Shipped with Ice Packs
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Description
Recombinant GroEL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-548) and having a molecular mass of 57.3kDa. GroEL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The groEL protein contains 25mM Tris buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GroEL protein is the major heat shock protein of E.coli and belongs to the chaperonin (HSP60) family. GroEL protein prevents misfolding of proteins and promotes the refolding and proper assembly of unfolded polypeptiedes generated under stress condition.
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Synonyms
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREIELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGIDKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDGTGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAVAKAGKPLLII AEDVEGEALA TAVVNTIRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTVISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDYDREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALIRVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNAATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM.
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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Name :
GTSF1 HumanDescription:
Gametocyte Specific Factor 1 Human Recombinant
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
Product # :
PRO-561Price :
Quantity :
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Shipped with Ice Packs
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Description
GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.
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Synonyms
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.
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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Name :
REG1A HumanDescription:
Regenerating Islet-Derived 1 Alpha Human Recombinant
Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.
Product # :
PRO-289Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human REG 1 alpha is produced with N-terminal fusion His Tag. The Recombinant Human REG 1 alpha His-Tagged Fusion Protein, has a molecular weight of 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 alpha and 12 additional amino acid residues – His Tag.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 5mM Tris, 25mM NaCl, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.
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Stability
Store lyophilized protein 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.
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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.
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Amino Acid Sequence
MKHHHHHHAS HMQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN.
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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Name :
RELM g MouseDescription:
RELM-Gamma Mouse Recombinant
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
Product # :
CYT-1035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
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Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized RELM g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM g Mouse 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.
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Solubility
It is recommended to reconstitute the lyophilized RELM g in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.
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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Name :
Protein-A/G CysDescription:
Protein A/G Cys Recombinant
Product # :
PRO-1928Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page, HPLC
Description
Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-A/G was lyophilized without any additives.
Purity
Greater than 96.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.sds-page, HPLC
More Info
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Introduction
The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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.
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Solubility
It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEC.
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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Name :
AGA Human, sf9Description:
Aspartylglucosaminidase Human Recombinant, sf9
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
Product # :
ENZ-990Price :
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Shipping Method :
Shipped with Ice Packs
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Description
AGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (24-346 a.a.) and having a molecular mass of 35.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-57kDa). AGA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AGA 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.
More Info
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Introduction
Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.
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Synonyms
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCIHHHH 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.
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Name :
KLK13 Human, sf9Description:
Kallikrein-13 Human Recombinant, sf9
Kallikrein-Related Peptidase 13, KLKL4, Kallikrein-Like Protein 4, Kallikrein 13, KLK-L4, Kallikrein-Like Gene 4, Kallikrein-13, EC 3.4.21.-, EC 3.4.21, Kallikrein-13.
Product # :
ENZ-911Price :
Quantity :
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Shipped with Ice Packs
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Description
KLK13 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (17-277a.a.) and having a molecular mass of 29.7kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). KLK13 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK13 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 8,000 pmol/min/ug. One unit will hydrolyze 1.0 pmole of BAEE to Na-Benzoyl-L-arginine per minute at pH8.0 at 25C.More Info
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Introduction
Kallikreins are a subgroup of serine proteases having various physiological functions. Many kallikreins are implicated in carcinogenesis and some have potential of becoming novel cancer and other disease biomarkers. Kallikrein-13 (KLK13) is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK13 gene expression is regulated by steroid hormones and may be useful as a marker for breast cancer.
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Synonyms
Kallikrein-Related Peptidase 13, KLKL4, Kallikrein-Like Protein 4, Kallikrein 13, KLK-L4, Kallikrein-Like Gene 4, Kallikrein-13, EC 3.4.21.-, EC 3.4.21, Kallikrein-13.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
GGVSQESSKV LNTNGTSGFL PGGYTCFPHS QPWQAALLVQ GRLLCGGVLV HPKWVLTAAH CLKEGLKVYL GKHALGRVEA GEQVREVVHS IPHPEYRRSP THLNHDHDIM LLELQSPVQL TGYIQTLPLS HNNRLTPGTT CRVSGWGTTT SPQVNYPKTL QCANIQLRSD EECRQVYPGK ITDNMLCAGT KEGGKDSCEG DSGGPLVCNR TLYGIVSWGD FPCGQPDRPG VYTRVSRYVL WIRETIRKYE TQQQKWLKGP QHHHHHH.
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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Name :
Leptin N82K Human, PEGDescription:
Leptin N82K Human Recombinant, Pegylated
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1107Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.
More Info
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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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.
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Solubility
It is recommended to reconstitute the lyophilized Pegylated Leptin 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.
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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Name :
MGAT2 Human, Sf9Description:
Mannoside Acetylglucosaminyltransferase 2 Human Recombinant, Sf9
Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.
Product # :
ENZ-1077Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MGAT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 427 amino acids (30-447a.a.) and having a molecular mass of 49.3kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MGAT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MGAT2 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 7.5), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.
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Synonyms
Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.
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Physical Appearance
Sterile filtered colorless solution.
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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
ADPRQRKNEA LAPPLLDAEP ARGAGGRGGD HPSVAVGIRR VSNVSAASLV PAVPQPEADN LTLRYRSLVY QLNFDQTLRN VDKAGTWAPR ELVLVVQVHN RPEYLRLLLD SLRKAQGIDN VLVIFSHDFW STEINQLIAG VNFCPVLQVF FPFSIQLYPN EFPGSDPRDC PRDLPKNAAL
KLGCINAEYP DSFGHYREAK FSQTKHHWWW KLHFVWERVK ILRDYAGLIL FLEEDHYLAP DFYHVFKKMW KLKQQECPEC DVLSLGTYSA SRSFYGMADK VDVKTWKSTE HNMGLALTRN AYQKLIECTD TFCTYDDYNW DWTLQYLTVS CLPKFWKVLV PQIPRIFHAG DCGMHHKKTC
RPSTQSAQIE SLLNNNKQYM FPETLTISEK FTVVAISPPR KNGGWGDIRD HELCKSYRRL QHHHHHH.
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.
- View Data Sheet
Name :
NECTIN3 HumanDescription:
Nectin Cell Adhesion Molecule 3 Human Recombinant
Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3.
Product # :
PRO-2504Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
NECTIN3 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 355 amino acids (58-404 a.a.) and having a molecular mass of 39.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
NECTIN3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
NECTIN3, also known as Nectin Cell Adhesion Molecule 3, is part of the nectin family. NECTIN3 is intended to initiate cell-cell adhesion to stimulate cell attachment and to allow subsequent formation of JAM-and cadherin-based intercellular junctions. NECTIN3 induces endocytosis-mediated down-regulation of PVR from the cell surface, which results in reduction of cell movement & proliferation. Following Nectin-3 activity adds strength to the junction through trans-interaction with various molecules.
-
Synonyms
Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3.
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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
GPIIVEPHVT AVWGKNVSLK CLIEVNETIT QISWEKIHGK SSQTVAVHHP QYGFSVQGEY QGRVLFKNYS LNDATITLHN IGFSDSGKYI CKAVTFPLGN AQSSTTVTVL VEPTVSLIKG PDSLIDGGNE TVAAICIAAT GKPVAHIDWE GDLGEMESTT TSFPNETATI ISQYKLFPTR FARGRRITCV VKHPALEKDI RYSFILDIQY APEVSVTGYD GNWFVGRKGV NLKCNADANP PPFKSVWSRL DGQWPDGLLA SDNTLHFVHP LTFNYSGVYI CKVTNSLGQR SDQKVIYISD PPTTTTLQPT IQWHPSTADI EDLATEPKKL PFPLSTLATI KDDTIATLEH 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.
- View Data Sheet
Name :
Leptin SalamanderDescription:
Leptin Salamander Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
Product # :
CYT-704Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Salamander Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of 16kDa. The Salamander Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Salamander Leptin was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
By inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity in that test is similar to that of mouse leptin.
More Info
-
Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized recombinant salamander leptin although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of recombinant salamander leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization recombinant salamander leptin can be stored at +4C for at least two weeks.
-
Solubility
It is recommended to reconstitute the lyophilized Salamander Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the ten N-terminal amino acids was determined and was found to be Ala-Ile-Met-Val-Asp-Gln-Leu-Arg-Met-Asp.
-
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.104 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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.
- View Data Sheet
Name :
TXN1 E.ColiDescription:
Thioredoxin E.Coli Recombinant
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
Product # :
PRO-334Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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- More Info
Description
Recombinant Thioredoxin was purified from E. coli harboring its gene.
Source
Escherichia Coli.
Formulation
Each mg of protein contains 20mM phosphate buffer pH 7.4.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
TRX activity is assayed by measuring the change in absorbance at 650 nm at 25°C using 0.13µM bovine insulin containing 0.33mM DTT (pH 6.5).
The specific activity was found to be 3IU/mg.More Info
-
Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase.Its Molecular Weight is 11.9kDa. and the pI is 4.67.
-
Synonyms
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
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Physical Appearance
Sterile Lyophilized Powder.
-
Stability
TRX although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized TRX in sterile 18MΩ-cm H2O.
-
Amino Acid Sequence
HMSDKIIHL TDDSFDTDVLKADGAIL VDFW AEWCGPCKMIAPILDEI GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGAL DANLA.
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.
- View Data Sheet
Description:
Fibronectin, Oryza Human Recombinant
Product # :
PRO-2841Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Fibronectin Human Recombinant is a single, non-glycosylated polypeptide chain having a molecular mass of 216kDa. The Fibronectin is purified by proprietary chromatographic techniques.
Source
Oryza sativa (rice).
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin 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 Fibronectin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism mainly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.
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.
- View Data Sheet
Name :
KLK3 Human, HEKDescription:
Kallikrein-3 Human Recombinant, HEK
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1
Product # :
ENZ-1149Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLK3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (18-261 a.a) containing a total of 250 amino acids, having a molecular mass of 27.6kDa.KLK3 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The KLK3 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 250pmol/min/ug. Defined by the amount of enzyme that cleaves 1pmole of Succinyl-ArgPro-Tyr-p-Nitroanilide to Succinyl-Arg-Pro-Tyr and p-Nitroanilide per minute at pH 7.5 at 37˚C.
More Info
-
Introduction
Kallikrein-3 or KLK3 is a serine proteases subgroup, enzymes can cleave peptide bonds. KLK3 is found in the prostate and may be hold accountable to the regulation of semen liquefaction via seminogelin hydrolysis. The protein is expressed in low concentrations in men with healthy prostates serum. When elevated quantities are found it may show prostate cancer or different prostate disorders such as prostatitis and benign prostatic hyperplasia.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1
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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.
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Amino Acid Sequence
APLILSRIVG GWECEKHSQP WQVLVASRGR AVCGGVLVHP QWVLTAAHCI RNKSVILLGR HSLFHPEDTG QVFQVSHSFP HPLYDMSLLK NRFLRPGDDS SHDLMLLRLS EPAELTDAVK VMDLPTQEPA LGTTCYASGW GSIEPEEFLT PKKLQCVDLH VISNDVCAQV HPQKVTKFML CAGRWTGGKS TCSGDSGGPL VCNGVLQGIT SWGSEPCALP ERPSLYTKVV HYRKWIKDTI VANPHHHHHH
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.
- View Data Sheet
Name :
EREG HumanDescription:
Epiregulin Human Recombinant
EREG, Epiregulin, ER.
Product # :
CYT-609Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.More Info
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Introduction
Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.
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Synonyms
EREG, Epiregulin, ER.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epiregulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epiregulin 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 Epiregulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 5.6kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.
What is the amino acid sequence of EREG Protein?
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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.
- View Data Sheet
Name :
S100G HumanDescription:
S100 Calcium Binding Protein G Human Recombinant
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
Product # :
PRO-156Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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- More Info
Description
The Recombinant Human S100G produced in E.coli has a molecular mass of 10.04kDa containing 87 amino acid residues of the human S100G and fused to a 9 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
S100G was filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
More Info
-
Introduction
S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.
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Synonyms
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
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Stability
Store lyophilized protein 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS TKKSPEELKRS TKKSPEELKR IFEKYAAKEG DPDQLSKDEL KLLIQAEFPS LLKGPNTLDD LFQELDKNGD GEVSFEEFQV LVKKISQ.
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Applications
Western blotting.
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.
- View Data Sheet
Name :
SCGN HumanDescription:
Secretagogin Human Recombinant
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.
Product # :
PRO-599Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
SCGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276 a.a.) and having a molecular mass of 34.2kDa. SCGN is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
SCGN His-Tag (1mg/ml) protein is supplied in 20mM Tris HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas. -
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.
-
Physical Appearance
Sterile Filtered colorless liquid formulation.
-
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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSSREPTLG RLDAAGFWQV WQRFDADEKG YIEEKELDAF FLHMLMKLGT DDTVMKANLH KVKQQFMTTQ DASKDGRIRM KELAGMFLSE DENFLLLFRR ENPLDSSVEF MQIWRKYDAD SSGFISAAEL RNFLRDLFLH HKKAISEAKL EEYTGTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DACSTEERKR DFEKIFAYYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCL GLKINP.
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.
- View Data Sheet
Name :
DCN HumanDescription:
Decorin Human Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.
Product # :
PRO-1583Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.
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.
- View Data Sheet
Name :
NECTIN2 HumanDescription:
Nectin Cell Adhesion Molecule 2 Human Recombinant
Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.
Product # :
PRO-2461Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
NECTIN2 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 337 amino acids (32-360a.a.) and having a molecular mass of 36.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN2 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
NECTIN2 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.
More Info
-
Introduction
Nectin Cell Adhesion Molecule 2, also known as NECTIN2, is a Ca(2+)-independent cell-cell adhesion molecule which is one of the plasma membrane components of adherens junctions. NECTIN2 takes a vital part in the establishment of homotypic as well as heterotypic cell to cell contacts. NECTIN2 is essential for resisting herpes simplex virus type 2 infection in transfected cells. NECTIN2 is also a possible target for antibody therapy of breast & ovarian cancers. NECTIN2 might be related with human longevity. Two diseases which have been associated with NECTIN2 are Herpes Simplex and Ovarian Cystic Teratoma.
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Synonyms
Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.
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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
QDVRVQVLPE VRGQLGGTVE LPCHLLPPVP GLYISLVTWQ RPDAPANHQN VAAFHPKMGP SFPSPKPGSE RLSFVSAKQS TGQDTEAELQ DATLALHGLT VEDEGNYTCE FATFPKGSVR GMTWLRVIAK PKNQAEAQKV TFSQDPTTVA LCISKEGRPP ARISWLSSLD WEAKETQVSG TLAGTVTVTS RFTLVPSGRA DGVTVTCKVE HESFEEPALI PVTLSVRYPP EVSISGYDDN WYLGRTDATL SCDVRSNPEP TGYDWSTTSG TFPTSAVAQG SQLVIHAVDS LFNTTFVCTV TNAVGMGRAE QVIFVRETPN TAGAGATGGL EHHHHHH.
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.
- View Data Sheet
Name :
Ecotin E.ColiDescription:
Ecotin E.Coli Recombinant
E. coli serine protease inhibitor.
Product # :
ENZ-058Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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Description
Ecotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (21-162a.a.) and having a molecular mass of 18.3kDa.Ecotin is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ecotin protein solution (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 50mM NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Ecotin inhibits pancreatic serine proteases. Ecotin protein inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The power of inhibition is not linked to a specific protease specificity.
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Synonyms
E. coli serine protease inhibitor.
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Physical Appearance
Sterile Filtered clear solution.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAESVQPLEK IAPYPQAEKG MKRQVIQLTP QEDESTLKVE LLIGQTLEVD CNLHRLGGKL ENKTLEGWGY DYYVFDKVSS PVSTMMACPD GKKEKKFVTA YLGDAGMLRY NSKLPIVVYT PDNVDVKYRV WKAEEKIDNA VVR
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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Name :
NRGN HumanDescription:
Neurogranin Human Recombinant
hng, RC3, Neurogranin, Ng, NRGN.
Product # :
CYT-293Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NRGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a.) and having a molecular mass of 10.0kDa (molecular size on SDS-PAGE will appear higher). NRGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NRGN protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH7.0), 30% glycerol 0.1mM PMSF and 1mM EDTA.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Neurogranin (NRGN) is a calmodulin-binding protein which is expressed solely in the brain, mainly in dendritic spines. NRGN is also taking part in the protein kinase C signaling pathway by being a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. NRGN binds to calmodulin in the absence of calcium. NRGN protein’s phosphorylation by protein kinase C lowers its binding ability.
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Synonyms
hng, RC3, Neurogranin, Ng, NRGN.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDCCTEN ACSKPDDDIL DIPLDDPGAN AAAAKIQASF RGHMARKKIK SGERGRKGPG PGGPGGAGVA RGGAGGGPSG D.
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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Name :
NTS Human, sf9Description:
Neurotensin Human Recombinant, sf9
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
Product # :
PRO-2374Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
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Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH 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.
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Name :
ENHO HumanDescription:
Energy Homeostasis Associated Human Recombinant
Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.
Product # :
PRO-1569Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).
Source
Escherichia Coli.
Formulation
ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.
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Synonyms
Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein 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.
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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. ENHO is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.
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.