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Name :
HK2 HumanDescription:
Hexokinase-2 Human Recombinant
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
Product # :
PKA-227Price :
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Shipped with Ice Packs
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Description
HK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-917) fused to a 20 His tag at the N-terminal encoding the sequence of 937 amino acids in total and having a molecular mass of 104.1 kDa.HXK2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl pH8.0 and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 3-4 units/ml obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. In the coupled mode, one unit will produce 1.0 umole of NADPH per minute as glucose is phosphorylated by ATP at pH 7.4 at 30C.More Info
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Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.
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Synonyms
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
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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). Please avoid freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL GFTFSFPCHQTKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDISDIEGEKDGIR KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKENKGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG KGAAMVTAVAYRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS KETHASAPVK MLPTYVCATPDGTEKGDFLA LDLGGTNFRV LLVRVRNGKW GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG AALITAVACR IREAGQR.
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 :
SELE Human, Sf9Description:
E-Selectin Human Recombinant, Sf9
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E
Product # :
PRO-2712Price :
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Description
SELE Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids (22-556 a.a) and having a molecular mass of 59.4kDa.SELE is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The SELE solution (0.5mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by the ability of the immobilized protein to support the adhesion of U937 human histiocytic lymphoma cells, which are added to human E-Seletin/CD62E coated plates 2ug/ml. This effect is > 40%.
More Info
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Introduction
E-selectin (SELE) is a part of a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. E-selectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
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Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E
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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
WSYNTSTEAM TYDEASAYCQ QRYTHLVAIQ NKEEIEYLNS ILSYSPSYYW IGIRKVNNVW VWVGTQKPLT EEAKNWAPGE PNNRQKDEDC VEIYIKREKD VGMWNDERCS KKKLALCYTA ACTNTSCSGH GECVETINNY TCKCDPGFSG LKCEQIVNCT ALESPEHGSL VCSHPLGNFS YNSSCSISCD RGYLPSSMET MQCMSSGEWS APIPACNVVE CDAVTNPANG FVECFQNPGS FPWNTTCTFD CEEGFELMGA QSLQCTSSGN WDNEKPTCKA VTCRAVRQPQ NGSVRCSHSP AGEFTFKSSC NFTCEEGFML QGPAQVECTT QGQWTQQIPV CEAFQCTALS NPERGYMNCL PSASGSFRYG SSCEFSCEQG FVLKGSKRLQ CGPTGEWDNE KPTCEAVRCD AVHQPPKGLV RCAHSPIGEF TYKSSCAFSC EEGFELHGST QLECTSQGQW TEEVPSCQVV KCSSLAVPGK INMSCSGEPV FGTVCKFACP EGWTLNGSAA RTCGATGHWS GLLPTCEAPT ESNIPHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DEFB118 HumanDescription:
Beta Defensin 118 Human Recombinant
Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.
Product # :
CYT-714Price :
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Description
DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.
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Synonyms
Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.
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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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.
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Background
Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications
Abstract:
Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. 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 BD118.Role in Innate Immunity:
BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.Therapeutic Implications:
Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.Conclusion:
Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.What is the molecular weight/Mw of DEFB118 Protein?
DEFB118 Protein has a total Mw of 13.8kDa.
What is the source or expression system of DEFB118 Protein?
Escherichia Coli.
What is the Purity of DEFB118 Protein?
DEFB118 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB118 Protein?
The biological functionality of DEFB118 Protein will be determined in the future.
What is the amino acid sequence of DEFB118 Protein?
MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.
What applications can DEFB118 Protein be used in?
DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB118 Protein?
The endotoxin level is minimal, DEFB118 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 :
HMGB3 HumanDescription:
High-Mobility Group Box 3 Human Recombinant
High Mobility Group Box 3, High-Mobility Group (Nonhistone Chromosomal) Protein 4, Non-Histone Chromosomal Protein, High Mobility Group Protein B3, High Mobility Group Protein 4, HMG-2a, HMG-4.
Product # :
PRO-1623Price :
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Shipped with Ice Packs
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Description
HMGB3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-180) and having a molecular mass of 22.8kDa.HMGB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HMGB3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
HMGB3 is a member of the high mobility group (HMG) protein superfamily. HMGB3 holds DNA-binding HMG box domains, as do HMG1 and HMG2, and like the rest of the HMG protein superfamily members has a vital part in DNA replication, transcription and nucleosome assembly.
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Synonyms
High Mobility Group Box 3, High-Mobility Group (Nonhistone Chromosomal) Protein 4, Non-Histone Chromosomal Protein, High Mobility Group Protein B3, High Mobility Group Protein 4, HMG-2a, HMG-4.
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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 MGSMAKGDPK KPKGKMSAYA FFVQTCREEH KKKNPEVPVN FAEFSKKCSE RWKTMSGKEK SKFDEMAKAD KVRYDREMKD YGPAKGGKKK KDPNAPKRPP SGFFLFCSEF RPKIKSTNPG ISIGDVAKKL GEMWNNLNDS EKQPYITKAA KLKEKYEKDV ADYKSKGKFD GAKGPAKVAR KKV.
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 :
SERPINA4 HumanDescription:
Kallistatin Human Recombinant
Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin) Member 4, PI4, KST, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 4, Peptidase Inhibitor 4, Kallikrein Inhibitor, Serpin A4, PI-4, Protease Inhibitor 4 (Kallistatin), Kallistatin, KLST, KAL, SERPINA4.
Product # :
PRO-2036Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SERPINA4 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Gln21-Pro427) containing a total of 417 amino acids, having a calculated molecular mass of 47.7kDa and fused to a 10 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
SERPINA4 was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline pH 7.4 and 5% (w/v) Trehalose.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallistatin (SERPINA4) inhibits human amidolytic and kininogenase activities of tissue kallikrein. This inhibition is attained by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and production of a small C-terminal fragment of the inhibitor as a result of cleavage at the reactive site by tissue kallikrein.
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Synonyms
Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin) Member 4, PI4, KST, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 4, Peptidase Inhibitor 4, Kallikrein Inhibitor, Serpin A4, PI-4, Protease Inhibitor 4 (Kallistatin), Kallistatin, KLST, KAL, SERPINA4.
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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. SERPINA4 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
QLHVEHDGES CSNSSHQQIL ETGEGSPSLK IAPANADFAF RFYYLIASET PGKNIFFSPL SISAAYAMLS LGACSHSRSQ ILEGLGFNLT ELSESDVHRG FQHLLHTLNL PGHGLETRVG SALFLSHNLK FLAKFLNDTM AVYEAKLFHT NFYDTVGTIQ LINDHVKKET RGKIVDLVSE LKKDVLMVLV NYIYFKALWE KPFISSRTTP KDFYVDENTT VRVPMMLQDQ EHHWYLHDRY LPCSVLRMDY KGDATVFFIL PNQGKMREIE EVLTPEMLMR WNNLLRKRNF YKKLELHLPK FSISGSYVLD QILPRLGFTD LFSKWADLSG ITKQQKLEAS KSFHKATLDV DEAGTEAAAA TSFAIKFFSA QTNRHILRFN RPFLVVIFST STQSVLFLGK VVDPTKPHHH HHHHHHH.
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 :
SHC1 HumanDescription:
SHC-Transforming Protein 1 Human Recombinant
SHC (Src homology 2 domain containing) transforming protein 1, SHC, SHCA, SH2 domain protein C1, SHC-transforming protein 3, SHC-transforming protein A, FLJ26504, p66.
Product # :
PRO-883Price :
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Shipped with Ice Packs
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Description
SHC1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 494 amino acids (1-474) and having a molecular mass of 53.8 kDa.The SHC1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SHC1 protein (1mg/ml) is supplied in 20mM Tris-HCl, pH-8, 2mM DTT, 200mM NaCl, 0.1mM PMSF and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SHC1 is a member of the SH2 domain family. SHC1 is vital to the regulation of apoptosis and drug resistance in mammalian cells. SHC1 is a signaling adapter which links activated growth factor receptors to signaling pathway. SHC1 is found in neural stem cells but not in mature neurons.
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Synonyms
SHC (Src homology 2 domain containing) transforming protein 1, SHC, SHCA, SH2 domain protein C1, SHC-transforming protein 3, SHC-transforming protein A, FLJ26504, p66.
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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 MNKLSGGGGR RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH PNDKVMGPGV SYLVRYMGCV EVLQSMRALD FNTRTQVTRE AISLVCEAVP GAKGATRRRK PCSRPLSSIL GRSNLKFAGM PITLTVSTSS LNLMAADCKQ IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL ECPEGLAQDV ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEEPPDHQYY NDFPGKEPPL GGVVDMRLRE GAAPGAARPT APNAQTPSHL GATLPVGQPV GGDPEVRKQM PPPPPCPAGR ELFDDPSYVN VQNLDKARQA VGGAGPPNPA INGSAPRDLF DMKPFEDALR VPPPPQSVSM AEQLRGEPWF HGKLSRREAE ALLQLNGDFL VRESTTTPGQ YVLTGLQSGQ PKHLLLVDPE GVVRTKDHRF ESVSHLISYH MDNHLPIISA GSELCLQQPV ERKL
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 :
DSTN HumanDescription:
Destrin Human Recombinant
Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.
Product # :
PRO-1137Price :
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Description
DSTN Human Recombinant produced in E. coli is a single polypeptide chain containing 173 amino acids (1-165) and having a molecular mass of 19.5 kDa.DSTN is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DSTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Actin depolymerizing factor (Destrin/DSTN) belongs to the ADF/Cofilin/destrin superfamily which has the ability to swiftly depolymerize F-Actin in a stoichiometric mode. The ADF family of proteins is responsible for enhancing the turnover rate of actin in vivo. Destrin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. DSTN functions in a pH-independent manner. DSTN is found in a variety of epithelial and endothelial cells, however it is virtually nonexistent in adult mouse heart and skeletal muscle cells. Destrin shares a 71% sequence homology with Cofilin, however the 2 proteins vary in their interaction with Actin.
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Synonyms
Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.
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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
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPVLEHHH 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 :
ARPC5 HumanDescription:
Actin Related Protein 2/3 Complex, Subunit 5 Human Recombinant
Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.
Product # :
PRO-145Price :
Quantity :
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Shipped with Ice Packs
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Description
ARPC5 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 171 amino acids (1-151 a.a.) and having a molecular mass of 18.4kDa. The ARPC5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARPC5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ARPC5 is a 151 amino acid subunit of the Arp2/3 complex. ARPC5 is believed to have a role in maintaining the integrity of Arp2/3. ARPC5 is a substrate for MAPKAPK-2 which, via phosphorylation of ARPC5, may participate in Arp2/3 regulatory functions and remodeling of the Actin cytoskeleton.
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Synonyms
Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.
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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 MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN SSAMLLQWHE KALAAGGVGS IVRVLTARKT V.
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 :
SNAI1 HumanDescription:
Snail Family Zinc Finger 1 Human Recombinant
Snail Family Zinc Finger 1, Protein Sna, Protein Snail Homolog 1, SNAH, Snail 1 (Drosophila Homolog), Zinc Finger Protein, Snail Homolog 1 (Drosophila), SLUGH2, SNA, SNAIL, SNAIL1, dJ710H13.1, Snail 1 Homolog, Snail 1 Zinc Finger Protein, Snail 1, Zinc Finger Protein, Snail Homolog 1, Zinc Finger Protein SNAI1.
Product # :
PRO-1759Price :
Quantity :
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Description
SNAI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids (1-264 a.a) and having a molecular mass of 31.5kDa.SNAI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNAI1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Snail homolog 1 (SNAI1) is involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. SNAI1 binds to 3 E-boxes of the E-cadherin gene promoter and represses its transcription. The nuclear protein encoded by SNAI1 is structurally identical to the Drosophila snail protein, and is considered as well to be vital for mesoderm formation in the developing embryo. At least two variants of a similar processed pseudogene have been found on chromosome 2. Among the diseases associated with SNAI1 are waardenburg syndrome type iid, and inappropriate adh syndrome.
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Synonyms
SnailFamily ZincFinger 1, Protein Sna, Protein Snail Homolog 1, SNAH, Snail 1 (Drosophila Homolog), Zinc Finger Protein, Snail Homolog 1 (Drosophila), SLUGH2, SNA, SNAIL, SNAIL1, dJ710H13.1, Snail 1 Homolog, Snail 1 Zinc Finger Protein, Snail 1, Zinc Finger Protein, Snail Homolog 1, Zinc Finger Protein SNAI1.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPRSFLV RKPSDPNRKP NYSELQDSNP EFTFQQPYDQ AHLLAAIPPP EILNPTASLP MLIWDSVLAP QAQPIAWASL RLQESPRVAE LTSLSDEDSG KGSQPPSPPS PAPSSFSSTS VSSLEAEAYA AFPGLGQVPK QLAQLSEAKD LQARKAFNCK YCNKEYLSLG ALKMHIRSHT LPCVCGTCGK AFSRPWLLQG HVRTHTGEKP FSCPHCSRAF ADRSNLRAHL QTHSDVKKYQ CQACARTFSR MSLLHKHQES GCSGCPR
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IDI1 HumanDescription:
Isopentenyl-Diphosphate Delta Isomerase 1 Human Recombinant
Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.
Product # :
ENZ-189Price :
Quantity :
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Description
IDI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-228) and having a molecular mass of 28.6kDa.IDI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The IDI1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Isopentenyl-diphosphate isomerase 1 (IDI1) belongs to the IPP isomerase type I family and is involved in cholesterol biosynthesis. IDI1 is a peroxisomally-localized enzyme which catalyzes the interconversion of isopentenyl diphosphate (IPP) to its highly electrophilic isomer, dimethylallyl diphosphate (DMAPP), which is the substrate for the sequential reaction that results in the synthesis of farnesyl diphosphate and, eventually, cholesterol. Peroxisomal deficiency diseases such as Zellweger syndrome and neonatal adrenoleukodystrophy show a reduction in IPP isomerase activity.
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Synonyms
Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.
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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 MMPEINTNHL DKQQVQLLAE MCILIDENDN KIGAETKKNC HLNENIEKGL LHRAFSVFLF NTENKLLLQQ RSDAKITFPG CFTNTCCSHP LSNPAELEES DALGVRRAAQ RRLKAELGIP LEEVPPEEIN YLTRIHYKAQ SDGIWGEHEI DYILLVRKNV
TLNPDPNEIK SYCYVSKEEL KELLKKAASG EIKITPWFKI IAATFLFKWW DNLNHLNQFV DHEKIYRM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IDO1 HumanDescription:
Indoleamine 2,3-Dioxygenase 1 Human Recombinant
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
Product # :
ENZ-807Price :
Quantity :
Shipping Method :
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Description
IDO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403a.a) and having a molecular mass of 47.7kDa. IDO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDO1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.
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Synonyms
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
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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 MGSMAHAMEN SWTISKEYHI DEEVGFALPN PQENLPDFYN DWMFIAKHLP DLIESGQLRE RVEKLNMLSI DHLTDHKSQR LARLVLGCIT MAYVWGKGHG DVRKVLPRNI AVPYCQLSKK LELPPILVYA DCVLANWKKK DPNKPLTYEN MDVLFSFRDG DCSKGFFLVS LLVEIAAASA IKVIPTVFKA MQMQERDTLL KALLEIASCL EKALQVFHQI HDHVNPKAFF SVLRIYLSGW KGNPQLSDGL VYEGFWEDPK EFAGGSAGQS SVFQCFDVLL GIQQTAGGGH AAQFLQDMRR YMPPAHRNFL CSLESNPSVR EFVLSKGDAG LREAYDACVK ALVSLRSYHL QIVTKYILIP ASQQPKENKT SEDPSKLEAK GTGGTDLMNF LKTVRSTTEK SLLKEG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IDS HumanDescription:
Iduronate 2-Sulfatase Human Recombinant
Iduronate 2-Sulfatase, Alpha-L-Iduronate Sulfate Sulfatase, SIDS, Iduronate 2-Sulfatase 14 KDa Chain, Iduronate 2-Sulfatase 42 KDa Chain, Hunter Syndrome, EC 3.1.6.13, MPS2, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase.
Product # :
ENZ-1005Price :
Quantity :
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Description
IDS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 533 amino acids (26-550a.a) and having a molecular mass of 60.3kDa. (Molecular size on SDS-PAGE will appear at approximately 35-70kDa). IDS is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IDS protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Iduronate 2-Sulfatase also known as IDS, belongs to the highly-conserved sulfatase family of enzymes which catalyze the hydrolysis of O-sulfate and N-salfate esters from a variety of substrates. IDS is essential for the lysosomal degradation of the glycosaminoglycans (GAG) heparan sulfate as well as dermatan sulfate. Furthermore, IDS hydrolyzes the 2-sulfate group of the IDS units of the GAG.
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Synonyms
Iduronate 2-Sulfatase, Alpha-L-Iduronate Sulfate Sulfatase, SIDS, Iduronate 2-Sulfatase 14 KDa Chain, Iduronate 2-Sulfatase 42 KDa Chain, Hunter Syndrome, EC 3.1.6.13, MPS2, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase.
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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
SETQANSTTD ALNVLLIIVD DLRPSLGCYG DKLVRSPNID QLASHSLLFQ NAFAQQAVCA PSRVSFLTGR RPDTTRLYDF NSYWRVHAGN FSTIPQYFKE NGYVTMSVGK VFHPGISSNH TDDSPYSWSF PPYHPSSEKY ENTKTCRGPD GELHANLLCP VDVLDVPEGT LPDKQSTEQA IQLLEKMKTS ASPFFLAVGY HKPHIPFRYP KEFQKLYPLE NITLAPDPEV PDGLPPVAYN PWMDIRQRED VQALNISVPY GPIPVDFQRK IRQSYFASVS YLDTQVGRLL SALDDLQLAN STIIAFTSDH GWALGEHGEW AKYSNFDVAT HVPLIFYVPG RTASLPEAGE KLFPYLDPFD SASQLMEPGR QSMDLVELVS LFPTLAGLAG LQVPPRCPVP SFHVELCREG KNLLKHFRFR DLEEDPYLPG NPRELIAYSQ YPRPSDIPQW NSDKPSLKDI KIMGYSIRTI DYRYTVWVGF NPDEFLANFS DIHAGELYFV DSDPLQDHNM YNDSQGGDLF QLLMPLEHHH 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.
- View Data Sheet
Name :
NMM HumanDescription:
Non-Muscle Myosin-II Regulatory Light Chain Human Recombinant
Non-Muscle Myosin-II Regulatory Light Chain, NMM.
Product # :
PRO-366Price :
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Description
Non-Muscle Myosin-II Regulatory Light Chain Human Recombinant full length expressed in E.coli.The NMM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NMM protein at 0.2mg/ml in 20mM HEPES-KOH, pH7, 50mM NaCl, 1mM EDTA and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Assayed for phosphorilation by MLCK.
More Info
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Introduction
Non muscle Myosins are required for cytokinesis at the end of cell division, when a contractile ring near the plasmalemma divides the cytoplasm of the daughter cells. They are involved in cytoplasmic streaming movements in tissues, and especially in activation of motile cells such as fibroblasts and macrophages. Activation of non-muscle myosin-II is achieved by phosphorylation of Ser33 in the motif KKRPQRATSN by a dedicated, Ca +2 Calmodulin regulated light chain kinase (MLCK).
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Synonyms
Non-Muscle Myosin-II Regulatory Light Chain, NMM.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS LGKNPTDAYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEATGTIQE DYLRELLTTM GDRFTDEEVD ELYREAPIDK KGNFNYIEFT RILKHGAKDK DD.
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 :
ATG3 HumanDescription:
Autophagy Related 3 Human Recombinant
APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.
Product # :
PRO-1987Price :
Quantity :
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Description
ATG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a) and having a molecular mass of 38.3kDa. ATG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATG3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.
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Synonyms
APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.
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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 MGSMQNVINT VKGKALEVAE YLTPVLKESK FKETGVITPE EFVAAGDHLV HHCPTWQWAT GEELKVKAYL PTGKQFLVTK NVPCYKRCKQ MEYSDELEAI IEEDDGDGGW VDTYHNTGIT GITEAVKEIT LENKDNIRLQ DCSALCEEEE DEDEGEAADM EEYEESGLLE TDEATLDTRK IVEACKAKTD AGGEDAILQT RTYDLYITYD KYYQTPRLWL FGYDEQRQPL TVEHMYEDIS QDHVKKTVTI ENHPHLPPPP MCSVHPCRHA EVMKKIIETV AEGGGELGVH MYLLIFLKFV QAVIPTIEYD YTRHFTM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IFNAR2 HumanDescription:
Interferon Alpha And Beta Receptor Subunit 2 Human Recombinant
Interferon alpha/beta receptor 2, IFNAR2, IFN-alpha binding protein, Interferon alpha binding protein, Type I interferon receptor 2, interferon alpha/beta receptor 2 isoform a, IFN-R-2, IFNABR, IFNARB, IFN-alpha-REC, IFN-R, IMD45.
Product # :
CYT-1167Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
IFNAR2 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 456 amino acids (27-243 a.a.) and having a molecular mass of 51.7kDa. IFNAR2 is fused to an 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IFNAR2 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 500 ng/ml and is measured by its binding ability in a functional ELISA with Human IFN-alpha 2 in the presence of Human IFN-alpha/beta R1.
SDS-PAGE
More Info
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Introduction
Interferon Alpha and Beta Receptor Subunit 2 or IFNAR2 is a protein, part of the class II cytokine receptor family. When different innate immune signaling transduction are activated, there is a rapid induction of type I IFNs because it has an intronless gene source. IFNAR2 is the main ligand and binds to the receptor. Once bind, stabilization occurs and a signaling compelx recptor is formed. IFNAR2 also takes part in the activation process of STAT proteins.
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Synonyms
Interferon alpha/beta receptor 2, IFNAR2, IFN-alpha binding protein, Interferon alpha binding protein, Type I interferon receptor 2, interferon alpha/beta receptor 2 isoform a, IFN-R-2, IFNABR, IFNARB, IFN-alpha-REC, IFN-R, IMD45.
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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
ISYDSPDYTD ESCTFKISLR NFRSILSWEL KNHSIVPTHY TLLYTIMSKP EDLKVVKNCA NTTRSFCDLT DEWRSTHEAY VTVLEGFSGN TTLFSCSHNF WLAIDMSFEP PEFEIVGFTN HINVMVKFPS IVEEELQFDL SLVIEEQSEG IVKKHKPEIK GNMSGNFTYI IDKLIPNTNY CVSVYLEHSD EQAVIKSPLK CTLLPPGQES ESAESAKLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
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Background
What is the molecular weight/Mw of IFNAR2 HUMAN Protein?
IFNAR2 HUMAN Protein has a total Mw of 51.7kDa.
What is the source or expression system of IFNAR2 HUMAN Protein?
Sf9, Baculovirus cells.
What is the Purity of IFNAR2 HUMAN Protein?
IFNAR2 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNAR2 HUMAN Protein?
The ED50 range ≤ 500 ng/ml and is measured by its binding ability in a functional ELISA with Human IFN-alpha 2 in the presence of Human IFN-alpha/beta R1.
What is the amino acid sequence of IFNAR2 HUMAN Protein?
ISYDSPDYTD ESCTFKISLR NFRSILSWEL KNHSIVPTHY TLLYTIMSKP EDLKVVKNCA NTTRSFCDLT DEWRSTHEAY VTVLEGFSGN TTLFSCSHNF WLAIDMSFEP PEFEIVGFTN HINVMVKFPS IVEEELQFDL SLVIEEQSEG IVKKHKPEIK GNMSGNFTYI IDKLIPNTNY CVSVYLEHSD EQAVIKSPLK CTLLPPGQES ESAESAKLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
What applications can IFNAR2 HUMAN Protein be used in?
IFNAR2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNAR2 HUMAN Protein?
The endotoxin level is minimal, IFNAR2 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.
- View Data Sheet
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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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.
- View Data Sheet
Name :
IFNGR1 HumanDescription:
IFN Gamma Receptor 1 Human Recombinant
IFNGR1, CD119, IFNGR, IMD27A, IMD27B, CDw119.
Product # :
CYT-1074Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IFNGR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 234 amino acids (18-245a.a.) and having a molecular mass of 26.6kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).IFNGR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IFNGR1 protein solution (1mg/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
IFNGR1 is a part of the hematopoietic cytokine receptor superfamily. IFNGR1 forms a site that is recognized by the extracellular domain of IFNGR2 by inducing the rapid dimerization of chains. IFNGR1 Plays an important role in the IFN-gamma pathway that is essential for the cellular response to infectious agents. IFNGR1 is expressed in a membrane-bound form in various cells, and is over-expressed in tumor cells.
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Synonyms
IFNGR1, CD119, IFNGR, IMD27A, IMD27B, CDw119.
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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
EMGTADLGPS SVPTPTNVTI ESYNMNPIVY WEYQIMPQVP VFTVEVKNYG VKNSEWIDAC INISHHYCNI SDHVGDPSNS LWVRVKARVG QKESAYAKSE EFAVCRDGKI GPPKLDIRKE EKQIMIDIFH PSVFVNGDEQ EVDYDPETTC YIRVYNVYVR MNGSEIQYKI LTQKEDDCDE IQCQLAIPVS SLNSQYCVSA EGVLHVWGVT TEKSKEVCIT IFNSSIKGHH HHHH.
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Background
What is the molecular weight/Mw of IFNGR1 HUMAN Protein?
IFNGR1 HUMAN Protein has a total Mw of 16.8kDa.
What is the source or expression system of IFNGR1 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFNGR1 HUMAN Protein?
IFNGR1 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNGR1 HUMAN Protein?
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.
What is the amino acid sequence of IFNGR1 HUMAN Protein?
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.
What applications can IFNGR1 HUMAN Protein be used in?
IFNGR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNGR1 HUMAN Protein?
The endotoxin level is minimal, IFNGR1 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.
- View Data Sheet
Name :
NRIP3 HumanDescription:
Nuclear Receptor-Interacting Protein 3 Human Recombinant
C11orf14, NY-SAR-105, Nuclear receptor-interacting protein 3, Sarcoma antigen NY-SAR-105, NRIP3.
Product # :
PRO-1384Price :
Quantity :
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Description
NRIP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-241 a.a.) and having a molecular mass of 29.4kDa. NRIP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NRIP3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Nuclear Receptor-Interacting Protein (NRIP3)is a 241 amino acid protein which is encoded by a gene that maps to human chromosome 11.Diseases associated with NRIP3 include sarcoma, and acute myeloid leukemia.
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Synonyms
C11orf14, NY-SAR-105, Nuclear receptor-interacting protein 3, Sarcoma antigen NY-SAR-105, NRIP3.
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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 MGSMFYSGLL TEGGRKETDM REAASLRQQR RMKQAVQFIH KDSADLLPLD GLKKLGSSKD MQPHNILQRR LMETNLSKLR SGPRVPWASK TNKLNQAKSE GLKKSEEDDM ILVSCQCAGK DVKALVDTGC LYNLISLACV DRLGLKEHVK SHKHEGEKLS LPRHLKVVGQ IEHLVITLGS LRLDCPAAVV DDNEKNLSLG LQTLRSLKCI INLDKHRLIM GKTDKEEIPF VETVSLNEDN TSEA.
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 :
SPAG7 HumanDescription:
Sperm Associated Antigen 7 Human Recombinant
ACRP, FSA-1, Sperm-associated antigen 7, SPAG7.
Product # :
PRO-1654Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPAG7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-227 a.a.) and having a molecular mass of 28kDa.SPAG7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SPAG7 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 7.5), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Sperm Associated Antigen 7 (SPAG7) is comprised of 1 R3H domain. SPAG7 is detected in fetal brain and localized in the nucleus.
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Synonyms
ACRP, FSA-1, Sperm-associated antigen 7, SPAG7.
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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 MGSMADLLGS ILSSMEKPPS LGDQETRRKA REQAARLKKL QEQEKQQKVE FRKRMEKEVS DFIQDSGQIK KKFQPMNKIE RSILHDVVEV AGLTSFSFGE DDDCRYVMIF KKEFAPSDEE LDSYRRGEEW DPQKAEEKRK LKELAQRQEE EAAQQGPVVV SPASDYKDKY SHLIGKGAAK DAAHMLQANK TYGCVPVANK RDTRSIEEAM NEIRAKKRLR QSGEELPPTS.
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 :
IGFLR1 HumanDescription:
IGF-Like Family Receptor 1 Human Recombinant
TMEM149, U2AF1L4, IGF-like family receptor 1, Transmembrane protein 149, U2 small nuclear RNA auxiliary factor 1-like 4, IGFLR1.
Product # :
PRO-1432Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IGFLR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (23-163) and having a molecular mass of 17.5kDa. IGFLR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The IGFLR1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GF-like family receptor 1 (IGFLR1) is encoded by a gene mapping to human chromosome 19. IGFLR1 which is cell membrane receptor for the IGF-like family proteins binds IGFL1 and IGFL3 with a higher affinity and may as well bind IGFL2.
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Synonyms
TMEM149, U2AF1L4, IGF-like family receptor 1, Transmembrane protein 149, U2 small nuclear RNA auxiliary factor 1-like 4, IGFLR1.
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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 MGSSQYCGRL EYWNPDNKCC SSCLQRFGPP PCPDYEFREN CGLNDHGDFV TPPFRKCSSG QCNPDGAELC SPCGGGAVTP TPAAGGGRTP WRCRERPVPA KGHCPLTPGN PGAPSSQERS SPASSIAWRT PEPVPQQAWP NFLP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NTS Human, sf9Description:
Neurotensin Human Recombinant, sf9
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
Product # :
PRO-2374Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
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Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SRP19 HumanDescription:
Signal Recognition Particle 19kDa Human Recombinant
Signal recognition particle 19kDa protein, SRP19.
Product # :
PRO-1474Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SRP19 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa. The SRP19 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRP19 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Signal recognition particle 19kDa protein (SRP19) is a member of the SRP19 family. SRP19 binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
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Synonyms
Signal recognition particle 19kDa protein, SRP19.
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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 MGSMACAAAR SPADQDRFIC IYPAYLNNKK TIAEGRRIPI SKAVENPTAT EIQDVCSAVG LNVFLEKNKM YSREWNRDVQ YRGRVRVQLK QEDGSLCLVQ FPSRKSVMLY AAEMIPKLKT RTQKTGGADQ SLQQGEGSKK GKGKKKK.
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 :
Omentin Human, HisDescription:
Omentin Human Recombinant, His Tag
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-551Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
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Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Intelectin His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin His Tag 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
MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.
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Applications
Elisa
Western blot.
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 :
IL 2 RatDescription:
Interleukin-2 Rat Recombinant
T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
Product # :
CYT-382Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
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- biological activity
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Description
Interleukin-2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 16kDa. The IL-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IL-2 solution contains 0.2µm filtered solution in 20mM PB pH3.5 and 30% Glycerol.
Purity
Greater than 97.0% as determined by SDS-PAGE and HPLC.
Biological Activity
The ED50 as determined by the dose-dependant stimulation of murine CTLL-2 cells is less than 0.2ng/ml, corresponding to a Specific Activity of 5,000,000IU/mg.
More Info
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Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
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Synonyms
T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
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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
APTSSPAKET QQHLEQLLLD LQVLLRGIDN YKNLKLPMML TFKFYLPKQA TELKHLQCLE NELGALQRVL DLTQSKSFHL EDAGNFISNI RVTVVKLKGS ENKFECQFDD EPATVVEFLR RWIAICQSII STMTQ.
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.