Search: 1000 results found for "Aprotinin"

Description:

HSP-70 Cofactor (HSP24) E.Coli Recombinant

HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

Product # :

HSP-014

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Description

GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

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Introduction
GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Synonyms
HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.
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
MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.

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:

Hypoxia-Inducible Factor-1 Alpha Human Recombinant, His Tag

Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

Product # :

PRO-415

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Description

HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (576-785 a.a.) and having a molecular mass of 25.1 kDa. The HIF1A is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HIF1A Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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 MSFDQLSPLE SSSASPESAS PQSTVTVFQQ TQIQEPTANA TTTTATTDEL KTVTKDRMED IKILIASPSP THIHKETTSA TSSPYRDTQS RTASPNRAGK GVIEQTEKSH PRSPNVLSVA LSQRTTVPEE ELNPKILALQ NAQRKRKMEH DGSLFQAVGI GTLLQQPDDH AATTSLSWKR VKGCKSSEQN GMEQKTIILI PSDLACRLLG Q.

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:

Secretagogin Rat Recombinant

SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.

Product # :

PRO-657

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Description

Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa. The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.The Rat SCGN is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile filtered concentrated protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

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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, Secretagogin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
Solubility
Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.

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-4 Human Recombinant (CCL13)

Small inducible cytokine A13, CCL13, Monocyte chemotactic protein 4, MCP-4, Monocyte chemoattractant protein 4, CK-beta-10, NCC-1, chemokine (C-C motif) ligand 13, NCC1, CKb10, SCYL1, SCYA13, MGC17134.

Product # :

CHM-319

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Description

Monocyte Chemotactic Protein-4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 75 amino acids and having a molecular mass of 8.6 kDa. The MCP-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution in 20mM PB, pH 7.4, 130mM NaCl.

Purity

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

Biological Activity

The specific activity as determined by the ability of MCP-4 to chemoattaract human monocytes at 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.

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Introduction
Chemokine (C-C motif) ligand 13 (CCL13 / MCP-4) is a small cytokine belonging to the CC chemokine family. The MCP-4 gene is located on human chromosome 17 within a large cluster of other CC chemokines. MCP-4 induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. Activity of the MCP-4 chemokine has been implicated in allergic reactions such as asthma. MCP-4 can be induced by the inflammatory cytokines interleukin-1 and TNF-a.
Synonyms
Small inducible cytokine A13, CCL13, Monocyte chemotactic protein 4, MCP-4, Monocyte chemoattractant protein 4, CK-beta-10, NCC-1, chemokine (C-C motif) ligand 13, NCC1, CKb10, SCYL1, SCYA13, MGC17134.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized MCP-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDALNVPSTCCFTFSSKKISLQRLKSYVITTSRCPQKAV
IFRTKLGKEICADPKEKWVQNYMKHLGRKAHTLKT.
Background
What is the molecular weight/Mw of CCL13 HUMAN Protein?
CCL13 HUMAN Protein has a total Mw of 8.6kDa.

What is the source or expression system of CCL13 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL13 HUMAN Protein?
CCL13 HUMAN Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL13 HUMAN Protein?
The specific activity as determined by the ability of MCP-4 to chemoattaract human monocytes at 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.

What is the amino acid sequence of CCL13 HUMAN Protein?
QPDALNVPSTCCFTFSSKKISLQRLKSYVITTSRCPQKAV
IFRTKLGKEICADPKEKWVQNYMKHLGRKAHTLKT.

What applications can CCL13 HUMAN Protein be used in?
CCL13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL13 HUMAN Protein?
The endotoxin level is minimal, CCL13 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL13 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL13 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Neutrophil Activating Protein-2 Human Recombinant (CXCL7)

Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

Product # :

CHM-274

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Description

Neutrophil Activating Protein-2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The NAP-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CXCL7 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

Greater than 97% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7should 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 Neutrophil Activating Protein-2in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.
Background
What is the molecular weight/Mw of CXCL7 HUMAN Protein?
CXCL7 HUMAN Protein has a total Mw of 7.6kDa.

What is the source or expression system of CXCL7 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL7 HUMAN Protein?
CXCL7 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL7 HUMAN Protein?
The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CXCL7 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.

What applications can CXCL7 HUMAN Protein be used in?
CXCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL7 HUMAN Protein?
The endotoxin level is minimal, CXCL7 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL7 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL7 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Carcinoembryonic Antigen Human

CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

Product # :

PRO-2801

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Description

CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.

Source

Liver tissue.

Formulation

CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
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.
Applications
Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.
Background
Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.
Structural Complexity of CEA:
CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.
CEA in Cancer Biology:
CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.
Beyond Cancer: CEA in Development and Inflammation:
While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.
CEA as a Diagnostic and Therapeutic Target:
The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.

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:

Non-Metastatic Cells 4 Human Recombinant, BioActive

Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.

Product # :

PRO-2642

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Description

NME4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa.NME4 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The NME4 solution (0.5mg/ml) contains 40% glycerol, 20mM Tris-HCl buffer (pH 8.0) and 0.2M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 120unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.

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Introduction
Non-Metastatic Cells 4 or NME4, is a nucleoside diphosphate kinase located in the mitochondria, and is part of the NDK family of proteins. NME4 ais a very common enzyme that enhances transfer of gamma-phosphates, through a phosphohistidine as a intermediate, between dioxynucleoside tri- and diphosphates. NME4 is originated from the nm23 gene. NME4 has a crucial part in the creation of nucleoside triphosphates that are not ATP.
Synonyms
Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.
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 MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA

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

Description:

Phosphoglycerate Kinase 1 Human Recombinant, BioActive

Phosphoglycerate kinase 1, MGC117307, MGC142128, MGC8947, MIG10, PGKA.

Product # :

PKA-124

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Description

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

Source

E.coli.

Formulation

The PGK1 solution (1mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0) and 1mM DTT.

.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity: > 600unit/mg. One unit will convert 1 umole of 1,3-Bisphosphoglycerate to 3-PGA per minute at pH 8.0 at 37C.

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Introduction
Phosphoglycerate kinase 1, also referred to PGK1, is an X-linked enzyme whichfunctions in the glycolytic pathway.The gene encoding the erythrocyte enzyme PGK1 & it seems that PGK-1 plays a role as a polymerase alpha cofactor protein (primer recognition protein) as a glyxolytic enzyme role. The PGK1 catalyzes the reversible conversion of 1, 3-diphosphoglycerate to 3-phosphoglycerate during glycolysis, generating one molecule of ATP.
Synonyms
Phosphoglycerate kinase 1, MGC117307, MGC142128, MGC8947, MIG10, PGKA.
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 MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI

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

Description:

Ubiquitin-Like Domain Containing CTD Phosphatase 1 Human Recombinant

CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.

Product # :

PRO-151

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Description

UBLCP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 39.2kDa.UBLCP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

UBLCP1 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation averts assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.
Synonyms
CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALPIIV KWGGQEYSVT TLSEDDTVLD LKQFLKTLTG VLPERQKLLG LKVKGKPAEN DVKLGALKLK PNTKIMMMGT REESLEDVLG PPPDNDDVVN DFDIEDEVVE VENREENLLK ISRRVKEYKV EILNPPREGK KLLVLDVDYT LFDHRSCAET GVELMRPYLH EFLTSAYEDY DIVIWSATNM KWIEAKMKEL GVSTNANYKI TFMLDSAAMI TVHTPRRGLI DVKPLGVIWG KFSEFYSKKN TIMFDDIGRN FLMNPQNGLK IRPFMKAHLN RDKDKELLKL TQYLKEIAKL DDFLDLNHKY WERYLSKKQG Q.

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:

Inositol Monophosphatase Domain Containing 1 Mouse Recombinant Bioactive

Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.

Product # :

PRO-2380

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Description

IMPAD1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (34-356a.a.) and having a molecular mass of 36.2kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). IMPAD1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IMPAD1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 5,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze Adenosine 3, 5-diphosphate per minute at pH 7.5 at 25C.

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Introduction
Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.
Synonyms
Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.
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
ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH HH.

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

Description:

RAD51D (1-328 a.a.) Human Recombinant

BROVCA4, R51H3, RAD51L3, TRAD, DNA repair protein RAD51 homolog 4, RAD51 homolog D, RAD51-like protein 3, RAD51D.

Product # :

PRO-1861

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Description

RAD51D (1-328) Human Recombinant produced in E. coli is. a single polypeptide chain containing 351 amino acids and having a molecular mass of 37.4kDa. RAD51D (1-328) is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RAD51D (1-328) solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
RAD51D is a member of the RAD51 protein family whose members are extremely similar to bacterial RecA and Saccharomyces cerevisiae Rad51. RAD51 protein family members take part in the homologous recombination and repair of DNA. RAD51D forms a complex with several other members of the RAD51 family which catalyzes homologous pairing between single- and double-stranded DNA, and participates in the early stage of recombinational repair of DNA.
Synonyms
BROVCA4, R51H3, RAD51L3, TRAD, DNA repair protein RAD51 homolog 4, RAD51 homolog D, RAD51-like protein 3, RAD51D.
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 MGSMGVLRVG LCPGLTEEMI QLLRSHRIKT VVDLVSADLE EVAQKCGLSY KALVALRRVL LAQFSAFPVN GADLYEELKT STAILSTGIG SLDKLLDAGL YTGEVTEIVG GPGSGKTQVC LCMAANVAHG LQQNVLYVDS NGGLTASRLL QLLQAKTQDE EEQAEALRRI QVVHAFDIFQ MLDVLQELRG TVAQQVTGSS GTVKVVVVDS VTAVVSPLLG GQQREGLALM MQLARELKTL ARDLGMAVVV TNHITRDRDS GRLKPALGRS WSFVPSTRIL LDTIEGAGAS GGRRMACLAK SSRQPTGFQE MVDIGTWGTS EQSATLQGDQ T.

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:

Cathelicidin Antimicrobial Peptide Human Recombinant

CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

Product # :

PRO-1405

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Description

CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.

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:

Dipeptidyl-Peptidase 4 Human Recombinant

CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

Product # :

ENZ-375

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Description

DPPIV Human Recombinant produced in Insect cells is a single, glycosylated polypeptide chain containing 737 amino acids (39-766) and having a molecular mass of 85.4kDa.DPPIV is fused to a 6 His Tag at C-terminus and purified using conventional chromatography techniques.

Source

Insect cells.

Formulation

DPP4 is formulated in 20mM Tris-HCl buffer pH-8, 100mM NaCl, 1mM EDTA and 10% glycerol.

Purity

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

Biological Activity

>200 Units/mg.

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Introduction
DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.
Synonyms
CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.
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
ADPSRKTYTL TDYLKNTYRL KLYSLRWISD HEYLYKQENN ILVFNAEYGN SSVFLENSTF DEFGHSINDY SISPDGQFIL LEYNYVKQWR HSYTASYDIY DLNKRQLITE ERIPNNTQWV TWSPVGHKLA YVWNNDIYVK IEPNLPSYRI TWTGKEDIIY NGITDWVYEE EVFSAYSALW WSPNGTFLAY AQFNDTEVPL IEYSFYSDES LQYPKTVRVP YPKAGAVNPT VKFFVVNTDS LSSVTNATSI QITAPASMLI GDHYLCDVTW ATQERISLQW LRRIQNYSVM DICDYDESSG RWNCLVARQH IEMSTTGWVG RFRPSEPHFT LDGNSFYKII SNEEGYRHIC YFQIDKKDCT FITKGTWEVI GIEALTSDYL YYISNEYKGM PGGRNLYKIQ LSDYTKVTCL SCELNPERCQ YYSVSFSKEA KYYQLRCSGP GLPLYTLHSS VNDKGLRVLE DNSALDKMLQ NVQMPSKKLD FIILNETKFW YQMILPPHFD KSKKYPLLLD VYAGPCSQKA DTVFRLNWAT YLASTENIIV ASFDGRGSGY QGDKIMHAIN RRLGTFEVED QIEAARQFSK MGFVDNKRIA IWGWSYGGYV TSMVLGSGSG VFKCGIAVAP VSRWEYYDSV YTERYMGLPT PEDNLDHYRN STVMSRAENF KQVEYLLIHG TADDNVHFQQ SAQISKALVD VGVDFQAMWY TDEDHGIASS TAHQHIYTHM SHFIKQCFSL PHHHHHH.
Unit Definition
One unit will hydrolyze 1 umole of p-nitroaniline per minute at pH8.0 at 37°C using 1mM of Gly-Pro p-nitroanilde as a substrate.

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:

Thrombin Human Recombinant, HEK

Prothrombin, EC 3.4.21.5, Coagulation factor II, F2, PT, THPH1, RPRGL2.

Product # :

PRO-1422

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Description

Recombinant Human Thrombin produced in HEK cells, having a total molecular weight of 36kDa. The Thrombin is purified by proprietary chromatographic techniques.

Source

HEK

Formulation

The Thrombin solution contains 20mM MES, pH6.0 and 500mM Choline Chloride.

Biological Activity

5396 NIH Units/mg.
The activity was determined in NIH units by comparing to Sigma’s human plasma thrombin. Protein concentration was measured using E(0.1%)@280nm = 1.83.

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Introduction
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
Synonyms
Prothrombin, EC 3.4.21.5, Coagulation factor II, F2, PT, THPH1, RPRGL2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store frozen at -20°C to -80°C for long periods of time. Avoid multiple freeze-thaw cycles.
Assay Conditions
Thrombin (1nM) was assayed using SPECTROZYME TH as a substrate (20µM) in 5mM Tris-HCl (pH8.0), 0.1% PEG, 200mM NaCl at 25°C.

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Description:

Actin, Alpha 2, Smooth Muscle, Aorta Human Recombinant

Actin Alpha 2 Smooth Muscle Aorta, Cell Growth-Inhibiting Gene 46 Protein, Actin Aortic Smooth Muscle, Alpha-Cardiac Actin, Alpha-Actin-2, MYMY5, ACTSA, ACTVS, AAT6.

Product # :

PRO-1220

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Description

ACTA2 Human Recombinant produced in E. coli is a single polypeptide chain containing 400 amino acids (3-377) and having a molecular mass of 44.4 kDa.ACTA2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ACTA2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
ACTA2 is a member of the actin family of proteins, an extremely conserved family of proteins which takes part in cell motility, structure and integrity. Three types of actin isoforms are known: Alpha, beta and gamma. Alpha actins are a main factor of the contractile mechanism, and beta and gamma take part in the regulation of cell motility. ACTA2 is an alpha actin which is located in skeletal muscle. Mutations in ACTA2 cause aortic aneurysm familial thoracic type 6. Various alternatively spliced variants, encoding the same protein were identified.
Synonyms
Actin Alpha 2 Smooth Muscle Aorta, Cell Growth-Inhibiting Gene 46 Protein, Actin Aortic Smooth Muscle, Alpha-Cardiac Actin, Alpha-Actin-2, MYMY5, ACTSA, ACTVS, AAT6.
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 MGSHMEEEDS TALVCDNGSG LCKAGFAGDD APRAVFPSIV GRPRHQGVMV GMGQKDSYVG DEAQSKRGIL TLKYPIEHGI ITNWDDMEKI WHHSFYNELR VAPEEHPTLL TEAPLNPKAN REKMTQIMFE TFNVPAMYVA IQAVLSLYAS GRTTGIVLDS GDGVTHNVPI YEGYALPHAI MRLDLAGRDL TDYLMKILTE RGYSFVTTAE REIVRDIKEK LCYVALDFEN EMATAASSSS LEKSYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVLSGGTTM YPGIADRMQK EITALAPSTM KIKIIAPPER KYSVWIGGSI LASLSTFQQM WISKQEYDEA GPSIVHRKCF.

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:

Integrin Binding Sialoprotein Human Recombinant, HEK

Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.

Product # :

PRO-2793

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Description

IBSP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain (17-317 a.a) containing a total of 307 amino acids and having a molecular mass of 34.3 kDa. IBSP is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

>40%, measured by the ability of the immobilized protein to support the adhesion of MCF7 human breast cancer cells. When cells are added to Human IBSP coated plates 3 ug/ml.

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Synonyms
Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.
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
FSMKNLHRRV KIEDSEENGV FKYRPRYYLY KHAYFYPHLK RFPVQGSSDS SEENGDDSSE EEEEEEETSN EGENNEESNE DEDSEAENTT LSATTLGYGE DATPGTGYTG LAAIQLPKKA GDITNKATKE KESDEEEEEE EEGNENEESE AEVDENEQGI NGTSTNSTEA ENGNGSSGGD NGEEGEEESV TGANAEDTTE TGRQGKGTSK TTTSPNGGFE PTTPPQVYRT TSPPFGKTTT
VEYEGEYEYT GANEYDNGYE IYESENGEPR GDNYRAYEDE YSYFKGQGYD GYDGQNYYHH QHHHHHH.
Background
1. Structural Diversity: Research on IBSP often delves into its structural characteristics. IBSP is known for its rich sialic acid content and multiple functional domains, including an RGD cell-binding domain and polyglutamic acid stretches. These structural features enable IBSP to interact with various cells, affecting adhesion and migration.
2. Mineralization Regulator: A significant focus of research is IBSP's role in mineralization. It acts as a nucleator for calcium phosphate crystals, providing a scaffold for bone formation. Understanding how IBSP influences mineralization is crucial for insights into bone health and diseases like osteoporosis.
3. Cell Signaling: Research papers explore IBSP's involvement in cell signaling pathways. IBSP has been linked to angiogenesis, inflammation, and cellular differentiation. Investigating these signaling pathways sheds light on its broader physiological roles.
4. Biomedical Implications: Studies often discuss the biomedical implications of IBSP. Researchers investigate its potential roles in bone disorders such as osteoporosis and periodontal disease. Additionally, IBSP's involvement in tumor metastasis and dental tissue regeneration is a subject of interest.
5. Recombinant IBSP: The use of recombinant IBSP in research is a significant topic. Researchers utilize recombinant IBSP to explore its functions, interactions, and potential therapeutic applications. This allows for controlled experiments and insights into IBSP's behavior.
6. Diagnostics and Therapeutics: Research papers may discuss the diagnostic and therapeutic potential of IBSP. Understanding its roles in health and disease can lead to the development of diagnostic markers and therapeutic interventions, particularly in the context of bone and dental health.
7. Clinical Relevance: Some research may focus on the clinical relevance of IBSP. This could include studies on patient populations with IBSP mutations or alterations, aiming to understand how variations in IBSP may contribute to specific medical conditions.

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:

Calmodulin Human

Calmodulin, CaM, CALM.

Product # :

PRO-2799

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Source

Human brain tissue.

Formulation

CALM was lyophilized with 2mM EDTA.

Purity

Greater than 95.0%.

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Synonyms
Calmodulin, CaM, CALM.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin 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 CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Applications
Blood samples from tissue donors were tested and found to be negative for syphilis, HBsAg, HIV-1 and HIV-2 antibodies and HCV.
Background
Calmodulin, a small, ubiquitous calcium-binding protein, stands as a linchpin in cellular signalling cascades. Its ability to modulate diverse cellular processes by transducing calcium signals has made it a focal point of scientific inquiry. With its role extending from muscle contraction to neurotransmitter release and gene expression, calmodulin orchestrates intricate physiological responses. This research delves into the multifaceted world of calmodulin, exploring its structural characteristics, calcium-binding properties, and its pivotal involvement in various biological pathways.
Structural Marvel of Calmodulin:
Calmodulin boasts a unique dumbbell-shaped structure, composed of four EF-hand motifs that enable it to bind calcium ions. When calcium binds to calmodulin, it undergoes a conformational change, allowing it to interact with a myriad of target proteins. This structural adaptability is fundamental to its ability to regulate a wide array of cellular activities.
Calcium Signalling and Transduction:
Intracellular calcium serves as a ubiquitous second messenger, and calmodulin is the key mediator of calcium signalling. When calcium levels rise, calmodulin binds calcium ions, triggering its activation. This activated form of calmodulin modulates the activity of various proteins, including enzymes, ion channels, and transcription factors. By doing so, calmodulin influences processes such as muscle contraction, neurotransmitter release, and cell proliferation.

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:

T-Complex 1 Human Recombinant

T-complex protein 1 subunit alpha, TCP-1-alpha, CCT-alpha, TCP1, CCT1, CCTA, D6S230E.

Product # :

PRO-276

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Description

TCP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 576 amino acids (1-556 a.a.) and having a molecular mass of 62.5kDa. The TCP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TCP1 solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT, 0.1mM PMSF and 10% Glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
TCP1 is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of 2 identical stacked rings, each containing eight different proteins. Unfolded polypeptides penetrate the central cavity of the complex and are folded in an ATP-dependent manner. The TCP1 protein is found in the cytosol as a subunit of a hetero-oligomeric chaperone. TCP1 has a significant function in maintaining cellular homoeostasis by assisting the folding of many proteins such as the cytoskeletal components actin and tubulin.
Synonyms
T-complex protein 1 subunit alpha, TCP-1-alpha, CCT-alpha, TCP1, CCT1, CCTA, D6S230E.
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 MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGSYEDAVH SGALND.

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:

Hepsin Human Recombinant

HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.

Product # :

PRO-2846

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Description

Hepsin Human Recombinant produced in Cho cells is a covalently-linked heterodimer having a total molecular mass of 43.0kDa. Hepsin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

The Hepsin protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The specific activity is >20,000 pmol/min/μg and was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC).

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Synonyms
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Hepsin Active although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hepsin Active 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 Hepsin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR.

Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H.
Background
Hepsin is a type II transmembrane serine protease expressed primarily on epithelial cells, it takes part in extracellular proteolysis by activating precursor proteins such as pro-HGF and contributes to tissue remodeling, cell signaling, and normal epithelial function. Recombinant Hepsin is used to study prostate cancer, extracellular matrix remodelling, protease signalling pathways, tumor invasion, metastasis, HGF/MET signaling, and for screening inhibitors that target serine proteases

What is the molecular weight / Mw of Hepsin Protein?
Hepsin Protein has a total Mw of 43kDa.

What is the source or expression system of Hepsin Protein?
CHO Cells

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

What is the Biological Activity of Hepsin Protein?
The enzymatic activity was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC). The specific activity is >20,000 pmol/min/μg.

What is the amino acid sequence of Hepsin Protein?
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H

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

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

Mannose-6-Phosphate Receptor (242-277) Human Recombinant

CD-MPR, MPR46, MPR 46, 46-KDa Mannose 6-Phosphate Receptor, MPR-46.

Product # :

PRO-2828

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Description

The M6PRHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The M6PRHis-Tagged Fusion Protein, produced in E. coli, is a 9kDa protein containing 36 amino acid residues of the M6PRHuman, 242-277 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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Synonyms
CD-MPR, MPR46, MPR 46, 46-KDa Mannose 6-Phosphate Receptor, MPR-46.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized M6PRat -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Mannose 6-phosphate receptors are membrane proteins which take part in the intracellular transport of lysosomal enzymes.
These receptors recognize and sort lysosomal hydrolases, facilitate their delivery to lysosomes via endocytic pathways.
M6PR binds to mannose 6-phosphate (M6P) residues on newly synthesized lysosomal enzymes in the Golgi apparatus, directing them to lysosomes.
After delivering enzymes to lysosomes, M6PRs are recycled back to the cell surface. This mechanism is critical for maintaining cellular homeostasis and efficient enzyme delivery.
M6PRs may also play a role in signaling pathways, influencing cellular responses to stress and metabolic changes.
Mutations or dysfunction in M6PRs can cause lysosomal storage disorders, emphasizing their importance in human health.
Recombinant M6PR has significant implications in therapeutic development, mainly in understanding lysosomal storage diseases and enhancing enzyme replacement therapies.

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:

CCAAT/enhancer binding protein CEBP Alpha Human Recombinant

CCAAT/enhancer-binding protein alpha, C/EBP alpha, CEBPA, CEBP.

Product # :

PRO-433

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Description

CEBP-a Human Recombinant His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 126 (aa 270-358) and having a molecular mass of 14.5 kDa. The Human CEBP-a Human is fused to a 37 amino acids His-Tag at N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CCAAT/enhancer binding protein(C/EBP) a is a family of transcription factors that all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and that form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBPs differ significantly in their physiological functions and in their downstream target genes. For example, mice lacking C/EBPa die shortly after birth due to severe hypoglycemia and the absence of glycogen storage in liver, whereas knockout of C/EBPb causes defects in female reproduction.
Synonyms
CCAAT/enhancer-binding protein alpha, C/EBP alpha, CEBPA, CEBP.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGAG KAKKSVDKNS NEYRVRRERN NIAVRKSRDK AKQRNVETQQ KVLELTSDND RLRKRVEQLS RELDTLRGIF RQLPESSLVKAMGNCA.

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:

R-Spondin-1 Human Recombinant

R-spondin-1, Cristin-3, mCristin-3, Roof plate-specific spondin-1, Rspo1, RSPO, R-spondin 1, R-spondin, Rspondin, CRISTIN3.

Product # :

PRO-2593

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Description

R-Spondin-1 Human Recombinant produced in CHO cells is a glycosylated monomer chain containing 243 amino acids and having a total molecular mass of 25.6kDa. RSPO1 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 Luciferase induction in HEK-293 STF cells in the presence of Murine Wnt-3a is 47.99ng/ml corresponding to a specific activity of 2.1 x 10^4 units/mg.

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Introduction
R-Spondin-1 (Rspo1) is a part of the Rspondin family. Rspo1 plays a role as an activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Rspo1 induces the onset of crypt cell proliferation and increases intestinal epithelial healing effect. Rspo1 is negatively regulating the TGF-beta pathway.
Synonyms
R-spondin-1, Cristin-3, mCristin-3, Roof plate-specific spondin-1, Rspo1, RSPO, R-spondin 1, R-spondin, Rspondin, CRISTIN3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized RSPO1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RSPO1 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 RSPO1in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SRGIKGKRQR RISAEGSQAC AKGCELCSEV NGCLKCSPKL FILLERNDIR QVGVCLPSCP PGYFDARNPD MNKCIKCKIE HCEACFSHNF CTKCKEGLYL HKGRCYPACP EGSSAANGTM ECSSPAQCEM SEWSPWGPCS KKQQLCGFRR GSEERTRRVL HAPVGDHAAC SDTKETRRCT VRRVPCPEGQ KRRKGGQGRR ENANRNLARK ESKEAGAGSR RRKGQQQQQQ QGTVGPLTSA GPA.

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:

Trafficking Protein Particle Complex 2-Like Human Recombinant

Trafficking protein particle complex subunit 2-like protein, TRAPPC2L.

Product # :

PRO-1543

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Description

TRAPPC2L Human Recombinant produced in E. coli is a single polypeptide chain containing 162 amino acids (1-139) and having a molecular mass of 18.4kDa. TRAPPC2L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TRAPPC2L solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Trafficking Protein Particle Complex 2-Like (TRAPPC2L) takes part in vesicular transport from endoplasmic reticulum to Golgi. TRAPPC2L is a part of the TRAPP small subunits family and is expressed in various organs like testis, liver, bladder, lung, spleen and brain.
Synonyms
Trafficking protein particle complex subunit 2-like protein, TRAPPC2L.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVCIAV IAKENYPLYI RSTPTENELK FHYMVHTSLD VVDEKISAMG KALVDQRELY LGLLYPTEDY KVYGYVTNSK VKFVMVVDSS NTALRDNEIR SMFRKLHNSY TDVMCNPFYN PGDRIQSRAF DNMVTSMMIQ VC.

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:

Microtubule-Associated Protein, RP/EB Family, Member 1 Human Recombinant

Microtubule-associated protein RP/EB family member 1, APC-binding protein EB1, End-binding protein 1, EB1, MAPRE1, MGC117374, MGC129946.

Product # :

PRO-058

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Description

MAPRE1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 288 amino acids (1-268 a.a.) and having a molecular mass of 32.2kDa. The MAPRE1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MAPRE1 solution (0.5 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
MAPRE1 (EB1) is a member of the intermediate/early gene family. MAPRE1 was first identified by its binding to the APC protein, which is often mutated in familial and sporadic, forms of colorectal cancer. MAPRE1 localizes to microtubules, especially the growing ends, in interphase cells. During mitosis, MAPRE1 is associated with the centrosomes and spindle microtubules. MAPRE1 is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes.
Synonyms
Microtubule-associated protein RP/EB family member 1, APC-binding protein EB1, End-binding protein 1, EB1, MAPRE1, MGC117374, MGC129946.
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 MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD GKDYDPVAAR QGQETAVAPS LVAPALNKPK KPLTSSSAAP QRPISTQRTA AAPKAGPGVV RKNPGVGNGD DEAAELMQQV NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ RIVDILYATD EGFVIPDEGG PQEEQEEY.

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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