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Name :
SIGLEC6 HumanDescription:
Sialic Acid Binding Ig Like Lectin 6 Human Recombinant
Sialic Acid Binding Ig Like Lectin 6, Obesity-Binding Protein 1, CD33 Antigen-Like 1, CDW327, CD33L1, CD33L, OBBP1, Sialic Acid Binding Ig-Like Lectin 6, Sialic Acid-Binding Ig-Like Lectin 6, CD327 Antigen, Siglec-6, CD33L2, OB-BP1, CD327, SIGLEC6.
Product # :
PRO-2450Price :
Quantity :
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Shipped with Ice Packs
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Description
SIGLEC6 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 563 amino acids (27-347a.a.) and having a molecular mass of 62.6kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC6 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SIGLEC6 protein solution (0.5mg/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
Sialic acid-binding Ig-like lectin 6 isoform 1 (SIGLEC6) is a member of immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC6 mediates sialic-acid dependent binding to cells and binds to alpha-2, 6-linked sialic acid. The SIGLEC6 protein localizes in numerous compartments such as membrane fraction, extracellular region and so on. The SIGLEC6 receptor binds sialyl-TN glycans and leptin. Placental expression SIGLEC6 is upregulated in preeclampsia.
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Synonyms
Sialic Acid Binding Ig Like Lectin 6, Obesity-Binding Protein 1, CD33 Antigen-Like 1, CDW327, CD33L1, CD33L, OBBP1, Sialic Acid Binding Ig-Like Lectin 6, Sialic Acid-Binding Ig-Like Lectin 6, CD327 Antigen, Siglec-6, CD33L2, OB-BP1, CD327, SIGLEC6.
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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
ADLQERRFQL EGPESLTVQE GLCVLVPCRL PTTLPASYYG YGYWFLEGAD VPVATNDPDE EVQEETRGRF HLLWDPRRKN CSLSIRDARR RDNAAYFFRL KSKWMKYGYT SSKLSVRVMA LTHRPNISIP GTLESGHPSN LTCSVPWVCE QGTPPIFSWM SAAPTSLGPR TTQSSVLTIT PRPQDHSTNL TCQVTFPGAG VTMERTIQLN VSYAPQKVAI SIFQGNSAAF KILQNTSSLP VLEGQALRLL CDADGNPPAH LSWFQGFPAL NATPISNTGV LELPQVGSAE EGDFTCRAQH PLGSLQISLS LFVHWKPEGR AGGVLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.
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 :
NENF HumanDescription:
Neudesin Neurotrophic Factor Human Recombinant
Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.
Product # :
CYT-778Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NENF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 32-172) containing 151 amino acids including a 10 a.a N-terminal His tag and having a molecular mass of 16.9kDa.
Source
Escherichia Coli.
Formulation
NENF was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Neudesin Neurotrophic Factor (NENF) is a member of the cytochrome b5 family, MAPR subfamily. NENF contains 1 cytochrome b5 heme-binding domain. NENF exhibits neurotrophic activity and activates phosphorylation of MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT in primary cultured neurons. NENF doesn’t have mitogenic activity in primary cultured astrocytes. NENF may play a part in neuronal differentiation and may have a transient influence on neural cell proliferation in neural precursor cells. NENF neurotrophic activity is increased by binding to heme. NENF is up-regulated in immortal cells and induced in estrogen receptor positive breast cancer expressing progesterone receptor.
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Synonyms
Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.
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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 0.5 mg/ml and let the lyophilized pellet dissolve completely. NENF 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
MKHHHHHHASGQTPRPAERG PPVRLFTEEE LARYGGEEED QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL TGKDSTRGVA KMSLDPADLT HDTTGLTAKE LEALDEVFTK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F.
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 :
EFNA5 HumanDescription:
Ephrin A5 Human Recombinant
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
Product # :
PRO-2327Price :
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Shipped with Ice Packs
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Description
EFNA5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 422 amino acids (21-203 a.a.) and having a molecular mass of 48.1kDa. EFNA5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNA5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.
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Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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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
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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 :
EG VEGF HumanDescription:
Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant
PK1, PRK1, Prokineticin 1, EG-VEGF.
Product # :
CYT-338Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
More Info
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Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
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Synonyms
PK1, PRK1, Prokineticin 1, EG-VEGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
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Background
Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications
Abstract:
Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent.Introduction:
Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders.Production and Characterization:
Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF.Role in Endocrine Disorders:
EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases.Therapeutic Implications:
Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies.Conclusion:
Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.7kDa.
What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.
What is the Purity of EG-VEGF Protein?
EG-VEGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EG-VEGF Protein?
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
What applications can EG-VEGF Protein be used in?
EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF 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.
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Name :
SOST MouseDescription:
Sclerostin Mouse Recombinant
SOST, Sclerostin, 5430411E23Rik.
Product # :
PRO-2670Price :
Quantity :
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Shipped with Ice Packs
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Description
SOST Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (24-211 a.a) containing 194 amino acids and having a molecular mass of 21.9 kDa.SOST is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
SOST protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
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Synonyms
SOST, Sclerostin, 5430411E23Rik.
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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
QGWQAFRNDA TEVIPGLGEY PEPPPENNQT MNRAENGGRP PHHPYDAKDV SEYSCRELHY TRFLTDGPCR SAKPVTELVC SGQCGPARLL PNAIGRVKWW RPNGPDFRCI PDRYRAQRVQ LLCPGGAAPR SRKVRLVASC KCKRLTRFHN QSELKDFGPE TARPQKGRKP RPGARGAKAN QAELENAYHH 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 :
ELP4 HumanDescription:
Elongator Acetyltransferase Complex Subunit 4 Human Recombinant
Elongator complex protein 4, ELP4, Elongator Acetyltransferase Complex Subunit 4, hELP4, PAX6 neighbor gene protein, C11orf19, PAXNEB, dJ68P15A.1, PAX6NEB.
Product # :
PRO-2102Price :
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Shipped with Ice Packs
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Description
ELP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424 a.a.) and having a molecular mass of 49kDa.ELP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ELP4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Elongator Acetyltransferase Complex Subunit 4, also known as ELP4 is a protein coding gene which is a subunit of the RNA polymerase II elongator complex. ELP4 complements phenotypes of yeast ELP4 deletion mutants and is related to Rolandic epilepsy.
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Synonyms
Elongator complex protein 4, ELP4, Elongator Acetyltransferase Complex Subunit 4, hELP4, PAX6 neighbor gene protein, C11orf19, PAXNEB, dJ68P15A.1, PAX6NEB.
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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 MGSMAAVATC GSVAASTGSA VATASKSNVT SFQRRGPRAS VTNDSGPRLV SIAGTRPSVR NGQLLVSTGL PALDQLLGGG LAVGTVLLIE EDKYNIYSPL LFKYFLAEGI VNGHTLLVAS AKEDPANILQ ELPAPLLDDK CKKEFDEDVY NHKTPESNIK MKIAWRYQLL PKMEIGPVSS SRFGHYYDAS KRMPQELIEA SNWHGFFLPE KISSTLKVEP CSLTPGYTKL LQFIQNIIYE EGFDGSNPQK KQRNILRIGI QNLGSPLWGD DICCAENGGN SHSLTKFLYV LRGLLRTSLS ACIITMPTHL IQNKAIIARV TTLSDVVVGL ESFIGSERET NPLYKDYHGL IHIRQIPRLN NLICDESDVK DLAFKLKRKL FTIERLHLPP DLSDTVSRSS KMDLAESAKR LGPGCGMMAG GKKHLDF.
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 :
ELP5 HumanDescription:
Elongator Acetyltransferase Complex Subunit 5 Human Recombinant
C17orf81, DERP6, HSPC002, MST071, MSTP071, Dermal papilla-derived protein 6, S-phase 2 protein, ELP5.
Product # :
PRO-1660Price :
Quantity :
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Shipped with Ice Packs
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Description
ELP5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-316 a.a.) and having a molecular mass of 37.2kDa.ELP5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ELP5 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Elongator acetyltransferase complex subunit 5 (ELP5) is a member of the ELP5 family. ELP5 functions as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is participated in transcriptional elongation. Elongator plays a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. ELP5 takes part in cell migration and is widely expressed in in heart, brain, liver, skeletal muscle and testis.
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Synonyms
C17orf81, DERP6, HSPC002, MST071, MSTP071, Dermal papilla-derived protein 6, S-phase 2 protein, ELP5.
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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 MGSMTPSEGA RAGTGRELEM LDSLLALGGL VLLRDSVEWE GRSLLKALVK KSALCGEQVH ILGCEVSEEE FREGFDSDIN NRLVYHDFFR DPLNWSKTEE AFPGGPLGAL RAMCKRTDPV PVTIALDSLS WLLLRLPCTT LCQVLHAVSH QDSCPGDSSS VGKVSVLGLL HEELHGPGPV GALSSLAQTE VTLGGTMGQA SAHILCRRPR QRPTDQTQWF SILPDFSLDL QEGPSVESQP YSDPHIPPVD PTTHLTFNLH LSKKEREARD SLILPFQFSS EKQQALLRPR PGQATSHIFY EPDAYDDLDQ EDPDDDLDI.
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 :
BEST1 HumanDescription:
Bestrophin 1 Human Recombinant
Bestrophin-1, TU15B, Vitelliform macular dystrophy protein 2, BEST1, VMD2, ARB, BEST, BMD, RP50, TU15B, Bestrophin-1 isoform 1, Bestrophin 1.
Product # :
PRO-1900Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BEST1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (292-585) and having a molecular mass of 36 kDa.BEST1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BEST1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Bestrophin 1 (BEST1) is a part of the bestrophin gene family and is also forms calcium-activated chloride-ion channels in epithelial. This small gene family is characterized by proteins with a highly conserved N-terminus with 4-6 transmembrane domains. BEST1 is extremely permeable to bicarbonate.
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Synonyms
Bestrophin-1, TU15B, Vitelliform macular dystrophy protein 2, BEST1, VMD2, ARB, BEST, BMD, RP50, TU15B, Bestrophin-1 isoform 1, Bestrophin 1.
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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 MGSEQLINPF GEDDDDFETN WIVDRNLQVS LLAVDEMHQD LPRMEPDMYW NKPEPQPPYT AASAQFRRAS FMGSTFNISL NKEEMEFQPN QEDEEDAHAG IIGRFLGLQS HDHHPPRANS RTKLLWPKRE SLLHEGLPKN HKAAKQNVRG QEDNKAWKLK AVDAFKSAPL YQRPGYYSAP QTPLSPTPMF FPLEPSAPSK LHSVTGIDTK DKSLKTVSSG AKKSFELLSE SDGALMEHPE VSQVRRKTVE FNLTDMPEIP ENHLKEPLEQ SPTNIHTTLK DHMDPYWALE NRDEAHS.
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 :
OLR1 HumanDescription:
Oxidized Low Density Lipoprotein Receptor 1 Human Recombinant
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1.
Product # :
PRO-923Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OLR1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (58-273) and having a molecular mass of 24.7 kDa.The OLR1 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The OLR1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
OLR1 is a type II membrane protein which belongs to the C-type lectin family and performs as a cell-surface receptor for Ox-LDL. Ox-LDL has a part in early ather-osclerosis, which includes the transformation of monocyte-derived macro-phages to foam cells in atherosclerotic lesions. In addition, OLR1 protein triggers the activation of the NF?B signal transduction pathway.
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Synonyms
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1.
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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
MQLSQVSDLL TQEQANLTHQ KKKLEGQISA RQQAEEASQE SENELKEMIE TLARKLNEKS KEQMELHHQN LNLQETLKRV ANCSAPCPQD WIWHGENCYL FSSGSFNWEK SQEKCLSLDA KLLKINSTAD LDFIQQAISY SSFPFWMGLS RRNPSYPWLW EDGSPLMPHL FRVRGAVSQT YPSGTCAYIQ RGAVYAENCI LAAFSICQKK ANLRAQ
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 :
EREG Human, HisDescription:
Epiregulin Human Recombinant, His Tag
Epiregulin, Proepiregulin, ER, ERP.
Product # :
CYT-859Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa. EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE
sds-page
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
Epiregulin, Proepiregulin, ER, ERP.
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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 MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 7.7kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The biological functionality of EREG Protein will be determined in the future.
What is the amino acid sequence of EREG Protein?
MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.
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.
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Name :
C19ORF80 HumanDescription:
Chromosome 19 Open Reading Frame 80 Human Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-1575Price :
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Description
C19ORF80 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-198) containing 187 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 21.1kDa (calculated).
Source
Escherichia Coli.
Formulation
C19ORF80 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
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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 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 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
MKHHHHHHASAPMGGPELAQ HEELTLLFHG TLQLGQALNG VYRTTEGRLT KARNSLGLYG RTIELLGQEV SRGRDAAQEL RASLLETQME EDILQLQAEA TAEVLGEVAQ AQKVLRDSVQ RLEVQLRSAW LGPAYREFEV LKAHADKQSH ILWALTGHVQ RQRREMVAQQ HRLRQIQERL HTAALPA.
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 :
C19ORF80 RatDescription:
Chromosome 19 Open Reading Frame 80 Rat Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-2024Price :
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Description
C19ORF80 Rat Recombinant produced in E. coli is a polypeptide chain containing 193 amino acids and having a total molecular mass of 22.0 kDa. C19ORF80 has a N-Terminal His-tag (10 AA residue).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from a 0.5mg/ml solution containing 0.03M Acetate buffer pH 4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
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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 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 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 VRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYKA TEARLTEAGR NLGLFDQALE FLGREVNQGR DATRELRTSL SEIQAEEDTL HLRAEATARS LREVARAQHA LRNSVRRLQV QLRGAWLGQA HQEFENLKDR ADKQNHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHMAA LPA
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 :
GADD45GIP1 HumanDescription:
Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant
Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.
Product # :
PRO-972Price :
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Description
GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.
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Synonyms
Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.
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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 MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS
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 :
TOMM20 HumanDescription:
Translocase Of Outer Mitochondrial Membrane 20 Human Recombinant
Mmitochondrial import receptor subunit TOM20 homolog, TOMM20, MAS20, MOM19, KIAA0016, Outer mitochondrial membrane receptor Tom20, Mitochondrial 20 kDa outer membrane protein.
Product # :
PRO-1471Price :
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Description
TOMM20 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (25-145) and having a molecular mass of 16.2 kDa. TOMM20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TOMM20 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Mmitochondrial import receptor subunit TOMM20 homolog (TOMM20) is a member of the Tom20 family. The Tom machinery consists of import receptors for the initial binding of cytosolically synthesized preproteins and a general import pore (GIP) for the membrane translocation of various preproteins into the mitochondria. TOMM20 acts as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.
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Synonyms
Mmitochondrial import receptor subunit TOM20 homolog, TOMM20, MAS20, MOM19, KIAA0016, Outer mitochondrial membrane receptor Tom20, Mitochondrial 20 kDa outer membrane protein.
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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 MGSDRKRRSD PNFKNRLRER RKKQKLAKER AGLSKLPDLK DAEAVQKFFL EEIQLGEELL AQGEYEKGVD HLTNAIAVCG QPQQLLQVLQ QTLPPPVFQM LLTKLPTISQ RIVSAQSLAE DDVE.
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 :
CETN1 HumanDescription:
Centrin-1 Human Recombinant
Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.
Product # :
PRO-1104Price :
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Description
CETN1 Human Recombinant produced E. coli is a single polypeptide chain containing 196 amino acids (1-172) and having a molecular mass of 22.1kDa.CETN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CETN1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.
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Synonyms
Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.
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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 MGSHMASGFK KPSAASTGQK RKVAPKPELT EDQKQEVREA FDLFDVDGSG TIDAKELKVA MRALGFEPRK EEMKKMISEV DREGTGKISF NDFLAVMTQK MSEKDTKEEI LKAFRLFDDD ETGKISFKNL KRVANELGEN LTDEELQEMI DEADRDGDGE VNEEEFLRIM KKTSLY
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 :
LILRB1 HumanDescription:
Leukocyte Immunoglobulin Like Receptor B1 Human Recombinant
Leukocyte immunoglobulin-like receptor subfamily B member 1,Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B
Product # :
PRO-2668Price :
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Description
LILRB1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (24-461 a.a) and having a molecular mass of 48.5kDa.LILRB1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The LILRB1 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
Biological activity is > 50%. It is defined by the ability of the immobilized protein to support the adhesion of HSB2 human peripheral blood acute lymphoblastic leukemia cells, while the cells are added to LILRB1 coated plates at 5ug/ml.
More Info
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Introduction
Leukocyte Immunoglobulin Like Receptor B1 (LILRB1) is a member of the leukocyteimmunoglobulinlike receptor (LIR) family. LILRB1is expressed on immune cells, binds to MHC classI molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immuneresponse. LILRB1 controls inflammatory responses and cytotoxicity to help focus the immune responseand limit autoreactivity. LILRB1 is also expressed on the surface of B cells and monocytes, subsets of NKcells, gamma δ T cells,memory/effector CD8+ T cells and monocyte-derived dendritic cells.
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Synonyms
Leukocyte immunoglobulin-like receptor subfamily B member 1,
Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B -
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
GHLPKPTLWA EPGSVITQGS PVTLRCQGGQ ETQEYRLYRE KKTAPWITRI PQELVKKGQF PIPSITWEHT GRYRCYYGSD TAGRSESSDP LELVVTGAYI KPTLSAQPSP VVNSGGNVTL QCDSQVAFDG FILCKEGEDE HPQCLNSQPH ARGSSRAIFS VGPVSPSRRW WYRCYAYDSN SPYEWSLPSD LLELLVLGVS KKPSLSVQPG PIVAPEETLT LQCGSDAGYN RFVLYKDGER DFLQLAGAQP QAGLSQANFT LGPVSRSYGG QYRCYGAHNL SSEWSAPSDP LDILIAGQFY DRVSLSVQPG PTVASGENVT LLCQSQGWMQ TFLLTKEGAA DDPWRLRSTY QSQKYQAEFP MGPVTSAHAG TYRCYGSQSS KPYLLTHPSD PLELVVSGPS GGPSSPTTGP TSTSGPEDQP LTPTGSDPQS GLGRHLGVLE HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LZIC HumanDescription:
Leucine Zipper And CTNNBIP1 Domain Containing Human Recombinant
WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.
Product # :
PRO-1831Price :
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Description
LZIC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (24-111) and having a molecular mass of 12.1 kDa. LZIC is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The LZIC solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
LZIC is a member of the CTNNBIP1 family. LZIC protein is universally expressed, with largest levels in kidney and up-regulated in various cases of gastric cancers. LZIC has no interaction with CTNNB1.
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Synonyms
WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.
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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 MGSMASRGKT ETSKLKQNLE EQLDRLMQQL QDLEECREEL DTDEYEETKK ETLEQLSEFN DSLKKIMSGN MTLVDELSGM QLAIQAAISQ AFKTPEVIRL FAKKQPGQLR TRLAEMDRDL MVGKLERDLY TQQKVEILTA LRKLGEKLTA DDEAFLSANA GAILSQFEKV STDLGSGDKI LALASFEVEK TKK.
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 :
LZTFL1 HumanDescription:
Leucine Zipper Transcription Factor-Like 1 Human Recombinant
Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.
Product # :
PRO-2157Price :
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Description
LZTFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 37.0kDa. LZTFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LZTFL1 protein solution (1mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Leucine Zipper Transcription Factor-Like 1, also known as LZTFL1 is a ubiquitously expressed protein which localizes to the cytoplasm. LZTFL1 interacts with Bardet-Biedl Syndrome proteins (BBS) and during its interaction with BBS protein complexes, regulates protein trafficking to the ciliary membrane. Nonsense mutations in LZTFL1 cause a form of Bardet-Biedl Syndrome; a ciliopathy characterized partly by polydactyly, obesity, cognitive impairment, hypogonadism, and kidney failure. LZTFL1 also acts as a tumor suppressor; possibly by interacting with E-cadherin as well as the actin cytoskeleton and in this manner regulating the transition of epithelial cells to mesenchymal cells.
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Synonyms
Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.
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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 MGSMAELGLN EHHQNEVINY MRFARSKRGL RLKTVDSCFQ DLKESRLVED TFTIDEVSEV LNGLQAVVHS EVESELINTA YTNVLLLRQL FAQAEKWYLK LQTDISELEN RELLEQVAEF EKAEITSSNK KPILDVTKPK LAPLNEGGTA ELLNKEILRL QEENEKLKSR LKTIEIQATN ALDEKSKLEK ALQDLQLDQG NQKDFIKAQD LSNLENTVAA LKSEFQKTLN DKTENQKSLE ENLATAKHDL LRVQEQLHMA EKELEKKFQQ TAAYRNMKEI LTKKNDQIKD LRKRLAQYEP ED.
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 :
Vaspin Human, HisDescription:
Vaspin Human Recombinant, His Tag
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Product # :
CYT-459Price :
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Description
Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.
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Synonyms
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Liquid Vaspin although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.
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 :
WHSC2 HumanDescription:
Wolf-Hirschhorn Syndrome Candidate 2 Human Recombinant
Negative elongation factor A, NELF-A, Wolf-Hirschhorn syndrome candidate 2 protein, WHSC2, NELFA, FLJ10442, FLJ25112, P/OKcl.15.
Product # :
PRO-062Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
WHSC2 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 559 amino acids (1-539 a.a.) and having a molecular mass of 60.6kDa. The WHSC2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The WHSC2 solution (0.25 mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
WHSC2 (NELF-A) is a protein factor required for DRB-sensitive transcription. WHSC2 is one of the 5 components of the multisubunit NELF complex which cooperates with DSIF to repress RNA polymerase II elongation. The Wolf-Hirschhorn syndrome is a multiple malformation syndrome characterized by mental and developmental defects resulting from a hemizygous deletion of the distal short arm of chromosome 4 (4p16.3).
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Synonyms
Negative elongation factor A, NELF-A, Wolf-Hirschhorn syndrome candidate 2 protein, WHSC2, NELFA, FLJ10442, FLJ25112, P/OKcl.15.
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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 MPGQRRALSP KMASMRESDT GLWLHNKLGA TDELWAPPSI ASLLTAAVID NIRLCFHGLS SAVKLKLLLG TLHLPRRTVD EMKGALMEII QLASLDSDPW VLMVADILKS FPDTGSLNLE LEEQNPNVQD ILGELREKVG ECEASAMLPL ECQYLNKNAL TTLAGPLTPP VKHFQLKRKP KSATLRAELL QKSTETAQQL KRSAGVPFHA KGRGLLRKMD TTTPLKGIPK QAPFRSPTAP SVFSPTGNRT PIPPSRTLLR KERGVKLLDI SELDMVGAGR EAKRRRKTLD AEVVEKPAKE ETVVENATPD YAAGLVSTQK LGSLNNEPAL PSTSYLPSTP SVVPASSYIP SSETPPAPSS REASRPPEEP SAPSPTLPAQ FKQRAPMYNS GLSPATPTPA APTSPLTPTT PPAVAPTTQT PPVAMVAPQT QAPAQQQPKK NLSLTREQMF AAQEMFKTAN KVTRPEKALI LGFMAGSREN PCQEQGDVIQ IKLSEHTEDL PKADGQGSTT MLVDTVFEMN YATGQWTRFK KYKPMTNVS.
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 :
REG4 HumanDescription:
Regenerating Islet-Derived 4 Human Recombinant
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
Product # :
PRO-424Price :
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Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human REG-4 is manufactured with N-terminal fusion of His Tag. The Recombinant Human REG-IV His-Tagged Fusion Protein is 17.4 kDa protein containing 136 amino acid residues of the Human REG 4 and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.
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
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
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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
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 HMDIIMRPSC APGWFYHKSN CYGYFRKLRN WSDAELECQS YGNGAHLASI LSLKEASTIA EYISGYQRSQ PIWIGLHDPQ KRQQWQWIDG AMYLYRSWSG KSMGGNKHCA EMSSNNNFLT WSSNECNKRQ HFLCKYRP.
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 :
Avidin RecombinantDescription:
Avidin Recombinant
Avidin, AVD, AVID.
Product # :
PRO-2597Price :
Quantity :
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Shipped at Room temp
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Description
Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.
Source
Corn (Zea Mays).
Purity
Greater than 90% as visualized by SDS-PAGE.
Biological Activity
13.5 units/mg protein, 1 unit binds 1µg biotin.
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Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
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Synonyms
Avidin, AVD, AVID.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Recombinant Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant Avidin 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 Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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 :
LysostaphinDescription:
Lysostaphin Recombinant
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
Product # :
ENZ-269Price :
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Shipping Method :
Shipped at Room temp
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Description
Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without any additives.
Purity
98% as determined by RP-HPLC.
Biological Activity
Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C. Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.
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Introduction
Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.
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Synonyms
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.
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Protein content
Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 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). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.
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Specific Activity
Determined to be 3,540 units/mg.
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 :
TRH HumanDescription:
Thyrotropin Releasing Hormone Human
Thyroliberin, TRH, MGC125964, MGC125965, Protirelin, TRF.
Product # :
HOR-264Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thyrotropin Releasing Hormone Human C16H22N6O4 has a molecular mass of 362.4 Dalton.The TRH is purified by proprietary chromatographic techniques.
Formulation
The TRH was lyophilized with no additives.
Purity
Greater than 98.2% as determined by analysis by RP-HPLC.
More Info
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Introduction
Thyrotropin-releasing hormone (TRH), also called thyrotropin-releasing factor (TRF), thyroliberin or protirelin, is a tripeptide hormonethat stimulates the release of thyroid-stimulating hormoneand prolactinby the anterior pituitary.
TRH is produced by the hypothalamus, near the paraventricular nucleus.
It travels across the median eminenceto the pituitary via the hypophyseal portal system. It is released from cells called thyrotropes.
In addition to the brain, TRH can also be detected in other areas of the body including the gastrointestinal systemand pancreatic islets.
Protirelin stimulates the secretion of pituitary thyroid stimulating hormone from the anterior pituitary and has been shown that protirelin increases secretion of prolactin. Protirelin is identified as 5-oxo-L-prolyl-L-histidyl-L-proline amide. It is a synthetic tripeptide that is believed to be structurally identical to the naturally-occurring thyrotropin-releasing hormone produced by the hypothalamus. -
Synonyms
Thyroliberin, TRH, MGC125964, MGC125965, Protirelin, TRF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protirelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRH 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 Thyroliberin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Pyr-His-Pro-NH2.
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Background
What is the molecular weight/Mw of TRH HUMAN Protein?
TRH HUMAN Protein has a total Mw of 0.36kDa.
What is the Purity of TRH HUMAN Protein?
TRH HUMAN Protein is >98.2% pure as determined by SDS-PAGE.
What is the Biological Activity of TRH HUMAN Protein?
The biological functionality of TRH HUMAN Protein will be determined in the future.
What is the amino acid sequence of TRH HUMAN Protein?
Pyr-His-Pro-NH2.
What applications can TRH HUMAN Protein be used in?
TRH HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TRH HUMAN Protein?
The endotoxin level is minimal, TRH HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.