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Description:

Adenosylmethionine Decarboxylase 1 Human Recombinant

Adenosylmethionine decarboxylase 1, S-adenosylmethionine decarboxylase proenzyme, AdoMetDC, S-adenosylmethionine decarboxylase 1, SAMDC, AMD, EC 4.1.1.50.

Product # :

ENZ-624

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Description

AMD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (68-334) and having a molecular mass of 33.4 kDa.AMD1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The AMD1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Adenosylmethionine decarboxylase proenzyme (AMD1) is synthesized originally as an inactive proenzyme. Putrescine stimulates both the proenzyme processing and the catalytic activity. The catalytic activity is inhibited by iodoacetic acid. The active enzyme formation entails a self-maturation process in which the active site pyruvoyl group is produced from an internal serine residue using an autocatalytic post-translational modification.
Synonyms
Adenosylmethionine decarboxylase 1, S-adenosylmethionine decarboxylase proenzyme, AdoMetDC, S-adenosylmethionine decarboxylase 1, SAMDC, AMD, EC 4.1.1.50.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
GSSHHHHHH SSGLVPRGSH MGSHMSSMFV SKRRFILKTC GTTLLLKALV PLLKLARDYS GFDSIQSFFY SRKNFMKPSH QGYPHRNFQE EIEFLNAIFP NGAAYCMGRM NSDCWYLYTL DFPESRVISQ PDQTLEILMS ELDPAVMDQF YMKDGVTAKD VTRESGIRDL IPGSVIDATM FNPCGYSMNG MKSDGTYWTI HITPEPEFSY VSFETNLSQT SYDDLIRKVV EVFKPGKFVT TLFVNQSSKC RTVLASPQKI EGFKRLDCQS AMFNDYNFVF TSFAKKQQQQ QS

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

Description:

Ankyrin Repeat Domain 54 Protein Human Recombinant

LIAR, Lyn-interacting ankyrin repeat protein.

Product # :

PRO-1480

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Description

ANKRD54 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a.) and having a molecular mass of 34.9kDa.ANKRD54 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ANKRD54 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Ankyrin Repeat Domain 54 (ANKRD54), which is also known as LIAR contains 4 ANK repeats. ANKRD54 plays a vital role in regulating intracellular signaling events related with erythroid terminal differentiation. ANKRD54 interacts with LYN through ankyrin repeat region and the SH3-domain in an activation-independent status of LYN. ANKRD54 creates a multiprotein complex with LYN and HCLS1.
Synonyms
LIAR, Lyn-interacting ankyrin repeat protein.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAAAGD ADDEPRSGHS SSEGECAVAP EPLTDAEGLF SFADFGSALG GGGAGLSGRA SGGAQSPLRY LHVLWQQDAE PRDELRCKIP AGRLRRAARP HRRLGPTGKE VHALKRLRDS ANANDVETVQ QLLEDGADPC AADDKGRTAL HFASCNGNDQ IVQLLLDHGA DPNQRDGLGN TPLHLAACTN HVPVITTLLR GGARVDALDR AGRTPLHLAK SKLNILQEGH AQCLEAVRLE VKQIIHMLRE YLERLGQHEQ RERLDDLCTR LQMTSTKEQV DEVTDLLASF TSLSLQMQSM EKR.

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

Description:

Actin Related Protein 2/3 Complex, Subunit 2 Human Recombinant

ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.

Product # :

PRO-1418

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Description

ARPC2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300a.a) and having a molecular mass of 36.7kDa. ARPC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

ARPC2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Actin-related protein 2/3 complex subunit 2 (ARPC2), is a part of the Rho family of small GTPases and one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. Nevertheless, the exact role of the protein (the p34 subunit) has yet to be determined.
Synonyms
ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMILLEVN NRIIEETLAL KFENAAAGNK PEAVEVTFAD FDGVLYHISN PNGDKTKVMV SISLKFYKEL QAHGADELLK RVYGSFLVNP ESGYNVSLLY DLENLPASKD SIVHQAGMLK RNCFASVFEK YFQFQEEGKE GENRAVIHYR DDETMYVESK KDRVTVVFST VFKDDDDVVI GKVFMQEFKE GRRASHTAPQ VLFSHREPPL ELKDTDAAVG DNIGYITFVL FPRHTNASAR DNTINLIHTF RDYLHYHIKC SKAYIHTRMR AKTSDFLKVL NRARPDAEKK EMKTITGKTF SSR.

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

Description:

Carbonic Anhydrase X Human Recombinant

Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.

Product # :

ENZ-1189

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Description

CA10 Human Recombinant is a single, glycosylated polypeptide chain containing 317 amino acids (22-328a.a) and having a molecular mass of 36.3kDa (calculated). CA10 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

CA10 protein solution (0.5mg/ml) is filtered in Phosphate-Buffered Saline pH 7.4 and 10% (w/v) glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH8.0 at 37℃.

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Synonyms
Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSMQQNSPK IHEGWWAYKE VVQGSFVPVP SFWGLVNSAW NLCSVGKRQS PVNIETSHMI FDPFLTPLRI NTGGRKVSGT MYNTGRHVSL RLDKEHLVNI SGGPMTYSHR LEEIRLHFGS EDSQGSEHLL NGQAFSGEVQ LIHYNHELYT NVTEAAKSPN GLVVVSIFIK VSDSSNPFLN RMLNRDTITR ITYKNDAYLL QGLNIEELYP ETSSFITYDG SMTIPPCYET ASWIIMNKPV YITRMQMHSL RLLSQNQPSQ IFLSMSDNFR PVQPLNNRCI RTNINFSLQG KDCPNNRAQK LQYRVNEWLL KHHHHHH
Background
Carbonic anhydrases (CAs) are a family of enzymes that play a crucial role in regulating pH balance and carbon dioxide transport in various tissues and organs. Carbonic anhydrase X (CA10) is a less-studied member of this family, and this research aims to explore its structure, function, and implications in metabolism and disease. Understanding the molecular mechanisms and regulatory roles of CA10 can provide valuable insights into its potential as a therapeutic target for various disorders.
Structure and Expression of Carbonic Anhydrase X:
CA10, also known as mitochondrial carbonic anhydrase, is a membrane-associated protein predominantly found in the mitochondria of various tissues, including the liver, kidney, and brain. It possesses the characteristic zinc-binding catalytic domain found in other CAs. However, CA10 has distinct features, including a unique N-terminal mitochondrial targeting sequence, suggesting its specific role within mitochondria.
Role of Carbonic Anhydrase X in Metabolism:
CA10 is involved in the regulation of pH and bicarbonate concentrations within the mitochondrial matrix, impacting mitochondrial metabolism. It catalyzes the reversible hydration of carbon dioxide to bicarbonate, facilitating the exchange of carbon dioxide between the mitochondria and the cytoplasm. This process is vital for maintaining acid-base homeostasis and efficient energy production through oxidative phosphorylation.
Implications of Carbonic Anhydrase X in Disease:
Emerging evidence suggests that CA10 may be implicated in various pathological conditions. Alterations in CA10 expression or activity have been associated with metabolic disorders, including obesity and diabetes. Furthermore, dysregulation of mitochondrial function and pH homeostasis, in which CA10 plays a role, have been linked to neurodegenerative diseases, cancer, and cardiovascular disorders. Elucidating the precise contributions of CA10 in these pathologies is an area of active investigation.
Therapeutic Potential of Carbonic Anhydrase X:
The unique properties and expression patterns of CA10 make it an intriguing target for therapeutic interventions. Modulating CA10 activity or expression could have implications in metabolic disorders, where the manipulation of mitochondrial function and pH regulation could offer therapeutic benefits. Developing selective inhibitors or activators of CA10 could be explored to regulate its enzymatic activity and modulate mitochondrial metabolism.
Challenges and Future Directions:
Although CA10 shows promise as a therapeutic target, several challenges remain. The elucidation of the precise regulatory mechanisms and signaling pathways involving CA10 within mitochondria is necessary for a comprehensive understanding of its function. Additionally, the development of specific modulators that selectively target CA10 without affecting other CAs or disrupting physiological processes is a critical consideration.
Conclusion:
The study of CA10 protein provides valuable insights into its distinct role in mitochondrial metabolism and disease pathogenesis. Understanding the molecular mechanisms and functional implications of CA10 opens avenues for the development of targeted therapies for metabolic disorders, neurodegenerative diseases, cancer, and cardiovascular disorders. Further research on CA10, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to improve patient outcomes.

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

Description:

Cadherin 5 Mouse Recombinant

Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.

Product # :

PRO-2244

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Description

CDH5 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 583 amino acids (25-599a.a.) and having a molecular mass of 66.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH5 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

CDH5 protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cadherin-5, also known as CDH5 is a classical cadherin which belongs to the cadherin superfamily. The CDH5is located in a six-cadherin cluster in a region on the long arm of chromosome 16 which is involved in loss ofheterozygosity events in breast as well as prostate cancer. CDH5 is a calcium-dependent cell-celladhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highlyconserved cytoplasmic tail. Furthermore, CDH5 functions as a classic cadherin by passing on to cells the ability to adhere in ahomophilic manner, CDH5 plays a significant role in endothelial cell biology through control of the cohesion as well as organization of the intercellular junctions.
Synonyms
Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
GPNFPQIDTP NMLPAHHRQK RDWIWNQMHI DEEKNESLPH YVGKIKSNVN RQNAKYVLQG EFAGKIFGVD ANTGNVLAYE RLDREKVSEY FLTALIVDKN TNKNLEQPSS FTVKVHDIND NWPVFSHQVF NASVPEMSAI GTSVIRVTAV DADDPTVAGH ATVLYQIVKG NEYFSIDNSG LIFTKIKNLD REKQAEYKIV VETQDALGLR GESGTATVMI RLEDINDNFP VFTQSTYTFS VPEDIRVGKP LGFLTVVDPD EPQNRMTKYS IMQGEYRDTF TIETDPKRNE GIIKPTKSLD YEVIQQYTFY IEATDPTIRY EYLSSTSGKN KAMVTINVLD VDEPPVFQRH FYHFKLPENQ KKPLIGTVVA KDPDKAQRSI GYSIRKTSDR GQFFRITKQG NIYNEKELDR ETYAWYNLTV EANELDSRGN PVGKESIVQV YIEVLDENDN PPEFAQPYEP KVCENAAQGK LVVQISATDK DVVPVNPKFK FALKNEDSNF TLINNHDNTA NITVKYGQFN REHAKFHYLP VLISDNGVPS LTGTSTLTVG VCKCNEQGEF TFCEEMAAQA GVSIQLEHHH 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.

Description:

ATP Synthase Subunit D, Mitochondrial Human Recombinant

ATP synthase subunit delta mitochondrial, F-ATPase delta subunit, ATP5D.

Product # :

ENZ-143

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Description

ATP5D produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (23-168 a.a.) and having a molecular mass of 17.3kDa.ATP5D is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ATP5D protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
F-ATPase delta (ATP5D) catalyzes ATP synthesis, employing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of 2 linked multi-subunit complexes: F1-the soluble catalytic core and Fo- the membrane-spanning component, which comprise the proton channel. The catalytic portion of mitochondrial ATP synthase consists of five different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alphas, 3 betas, and a single representative of the other three. The proton channel consists of three main subunits-a, b, c. ATP5D is the delta subunit of the catalytic core.
Synonyms
ATP synthase subunit delta mitochondrial, F-ATPase delta subunit, ATP5D.
Physical Appearance
Sterile filtered colorless solution.
Stability
ATP5D Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEAAAAPAA ASGPNQMSFT FASPTQVFFN GANVRQVDVP TLTGAFGILA AHVPTLQVLR PGLVVVHAED GTTSKYFVSS GSIAVNADSS VQLLAEEAVT LDMLDLGAAK ANLEKAQAEL VGTADEATRA EIQIRIEANE ALVKALE.

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

Description:

Apolipoprotein A-I Human Recombinant

Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.

Product # :

CYT-750

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Description

Apolipoprotein A-I Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 243 amino acids and having a molecular mass of 28.1kDa.The APOA1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The APOA1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

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Introduction
APOA1 (Apolipoprotein A-1) is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.
Synonyms
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Apolipoprotein A-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOA1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized APOA1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.
Background
Apolipoprotein A-I Human Recombinant: A Promising Therapeutic Agent for Cardiovascular Diseases
Abstract:

Cardiovascular diseases (CVDs) remain a leading cause of mortality worldwide. Dyslipidemia, characterized by abnormal lipid profiles, is a significant risk factor for the development of CVDs. Apolipoprotein A-I (ApoA-I) is the primary protein component of high-density lipoprotein (HDL), known as the "good cholesterol." ApoA-I plays a crucial role in reverse cholesterol transport, promoting the efflux of cholesterol from peripheral tissues to the liver for elimination. Recombinant ApoA-I offers a potential therapeutic strategy for enhancing HDL functionality and reducing CVD risk. This research paper aims to provide an overview of ApoA-I human recombinant, its production methods, and its therapeutic applications in cardiovascular medicine.
Introduction

Cardiovascular diseases and dyslipidemia
Role of apolipoprotein A-I in reverse cholesterol transport
Potential of ApoA-I human recombinant as a therapeutic agent
Structure and Function of Apolipoprotein A-I

Primary structure and domains of ApoA-I
Functional properties of ApoA-I in reverse cholesterol transport
Interaction with other lipoproteins and cellular receptors
Production of Apolipoprotein A-I Human Recombinant

Expression systems for recombinant ApoA-I
Biotechnological methods for large-scale production
Purification and characterization of recombinant ApoA-I
Therapeutic Applications of Apolipoprotein A-I Human Recombinant

Promotion of reverse cholesterol transport
Anti-inflammatory and antioxidant effects
Enhancement of endothelial function
Cardioprotective effects in animal models
Clinical Trials and Future Perspectives

Phase I and II clinical trials
Challenges and limitations
Future directions and potential therapeutic combinations
Conclusion

Summary of the potential of ApoA-I human recombinant as a therapeutic agent for CVDs
Importance of ongoing research and clinical trials
What is the molecular weight/Mw of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein has a total Mw of 28.1kDa.

What is the source or expression system of APOLIPOPROTEIN A1 Protein?
Escherichia Coli.

What is the Purity of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of APOLIPOPROTEIN A1 Protein?
The biological functionality of APOLIPOPROTEIN A1 Protein will be determined in the future.

What is the amino acid sequence of APOLIPOPROTEIN A1 Protein?
DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.

What applications can APOLIPOPROTEIN A1 Protein be used in?
APOLIPOPROTEIN A1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOLIPOPROTEIN A1 Protein?
The endotoxin level is minimal, APOLIPOPROTEIN A1 Protein was purified using conventional chromatography techniques.

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

Description:

Beta Defensin 116 Human Recombinant

Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.

Product # :

CYT-713

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Description

DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

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Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:

Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.
Introduction:

Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.
Production and Characterization:

Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.
Antimicrobial Properties:

BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.
Therapeutic Implications:

The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.
Conclusion:

Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.
What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.

What is the source or expression system of DEFB116 Protein?
Escherichia Coli.

What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.

What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 Protein was purified using conventional chromatography techniques.

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

Description:

Vascular Endothelial Growth Factor Mouse Recombinant, His Tag

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, Vegf120, Vegf164, Vegf188, Vegfa.

Product # :

CYT-680

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Description

VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (205-324 a.a.) and having a total molecular mass of 16.3kDa. Mouse VEGF is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse VEGF contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using NIH-3T3 mouse embryonic fibroblast. The ED50 for this effect is 0.5-1.5ng/ml.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, Vegf120, Vegf164, Vegf188, Vegfa.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKPR R.

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

Description:

WNT Inhibitory Factor 1 Mouse Recombinant

Wnt inhibitory factor 1, WIF-1, Wif1.

Product # :

PRO-2248

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Description

WIF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 359 amino acids (29-379a.a.) and having a molecular mass of 39.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).WIF1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

WIF1 protein solution (1mg/ml) contains 20mM MES (pH5.5), 1mM DTT, 1mM PMSF and 30% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.
Synonyms
Wnt inhibitory factor 1, WIF-1, Wif1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
GQPPEESLYL WIDAHQARVL IGFEEDILIV SEGKMAPFTH DFRKAQQRMP AIPVNIHSMN FTWQAAGQAE YFYEFLSLRS LDKGIMADPT VNVPLLGTVP HKASVVQVGF PCLGKQDGVA AFEVNVIVMN SEGNTILRTP QNAIFFKTCQ QAECPGGCRN GGFCNERRVC ECPDGFYGPH
CEKALCIPRC MNGGLCVTPG FCICPPGFYG VNCDKANCST TCFNGGTCFY PGKCICPPGL EGEQCELSKC PQPCRNGGKC IGKSKCKCPK GYQGDLCSKP VCEPGCGAHG TCHEPNKCQC REGWHGRHCN KRYGASLMHA PRPAGAGLER HTPSLKKAED RRDPPESNYI WVEHHHHHH.

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

Description:

Macrophage Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Product # :

CYT-431

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Description

MIF human Recombinant, fused to 40 a.a. His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques. Macrophage Inducing Factor Human Recombinant ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.

Source

Escherichia Coli.

Formulation

1mg/ml solution containing PBS pH-7.4.

Purity

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

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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Physical Appearance
Sterile filtered colorless solution.
Stability
Liquid MIF although stable 4°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.

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

Description:

Beta Defensin-4 Human Recombinant

HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.

Product # :

CYT-599

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Description

Beta Defensin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 50 amino acids and having a molecular mass of 6 kDa. The BD-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DEFB4 (1mg/ml) was lyophilized with 20mM sodium Phosphate buffer pH-7.4 and 130mM NaCl.

Purity

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

Biological Activity

Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.

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Introduction
Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.
Synonyms
HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-4 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Beta Defensin-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.
Background
Beta Defensin-4 Human Recombinant: Exploring the Potential of a Novel Antimicrobial Peptide
Abstract:
Beta Defensin-4 (hBD-4) human recombinant is a promising antimicrobial peptide with unique properties and potential therapeutic applications. This research paper provides an in-depth analysis of hBD-4, including its characteristics, mode of action, and potential uses. Furthermore, novel methodologies for the production and optimization of hBD-4 human recombinant are proposed, shedding light on its future implications in the field of infectious disease management.
Introduction:
In the face of increasing drug-resistant infections, alternative therapeutic strategies are crucial. Antimicrobial peptides, such as hBD-4, have gained attention due to their broad-spectrum activity against pathogens. This paper aims to explore the distinctive features of hBD-4 and propose innovative approaches for its production and optimization.
Characteristics and Mode of Action:
hBD-4 is a cationic peptide comprising 50 amino acids and is characterized by a unique structure that contributes to its antimicrobial properties. The mechanism of action involves the disruption of microbial membranes and subsequent cell death. Additionally, hBD-4 exhibits immunomodulatory effects, including the stimulation of chemotaxis and modulation of the inflammatory response.
Production of hBD-4 Human Recombinant:
Efficient production methodologies for hBD-4 human recombinant are essential for its therapeutic applications. Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents advantages and challenges, necessitating careful selection for high yields and protein quality. Optimization strategies, including codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-4 recombinant.
Potential Applications:
hBD-4 human recombinant demonstrates potential therapeutic applications in combating drug-resistant pathogens. Its broad-spectrum antimicrobial activity against bacteria, viruses, and fungi positions it as a promising candidate for infectious disease management. Moreover, hBD-4 shows promise in wound healing and tissue regeneration due to its ability to promote angiogenesis and stimulate cell migration. Exploring its potential in combination with drug delivery systems for targeted therapy is an exciting avenue for future research.
Conclusion:
hBD-4 human recombinant represents a novel antimicrobial peptide with diverse potential applications. Optimizing production methodologies and elucidating its mechanisms of action will further enhance its clinical utility. With its broad-spectrum antimicrobial activity and potential implications in wound healing and targeted therapy, hBD-4 human recombinant holds promise as an innovative therapeutic agent.
What is the molecular weight/Mw of BD4 Protein?
BD4 Protein has a total Mw of 6kDa.

What is the source or expression system of BD4 Protein?
Escherichia Coli.

What is the Purity of BD4 Protein?
BD4 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD4 Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.

What is the amino acid sequence of BD4 Protein?
EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.

What applications can BD4 Protein be used in?
BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD4 Protein?
The endotoxin level is minimal, BD4 Protein was purified using conventional chromatography techniques.

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

Description:

Betacellulin Human Recombinant

Product # :

CYT-330

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Description

Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Betacellulin Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized BTC Human in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
Background
Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine
Introduction
In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.
BTC: The Architect of Cellular Revitalization
BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.
Crafting the Alchemist: Pioneering Methodologies
Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.
Unveiling the Biological Tapestry
Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.
A Flourish of Results
The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.
Charting a Transformative Future
As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.
What is the molecular weight/Mw of BTC Protein?
BTC Protein has a total Mw of 9kDa.

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

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

What is the Biological Activity of BTC Protein?
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

What is the amino acid sequence of BTC Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

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

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

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

Description:

Leptin Quadruple Antagonist Pegylated Ovine Recombinant

Product # :

CYT-1246

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Description

Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 95.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

Ubiquitin Domain Containing 2 Human Recombinant

Ubiquitin domain containing protein 2, Dendritic cell-derived ubiquitin-like protein, Ubiquitin-like protein SB72, DCUBP, MGC30022.

Product # :

PRO-1203

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Description

UBTD2 Human Recombinant produced in E. coli is a single polypeptide chain containing 257 amino acids (1-234) and having a molecular mass of 28.6 kDa.UBTD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The UBTD2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
UBTD2 is an ubiquitin (Ub) domain-containing protein, originally recognized in dendritic cells, that takes part in ubiquitination pathway. Ubiquitin is the best understood post-translation modifier; however, there is a growing family of ubiquitin-like proteins (UBLs) who change cellular targets in a pathway. UbL proteins take part in a variation of cellular courses, like DNA repair, protein sorting, protein degradation, cell division, apoptosis and autophagy.
Synonyms
Ubiquitin domain containing protein 2, Dendritic cell-derived ubiquitin-like protein, Ubiquitin-like protein SB72, DCUBP, MGC30022.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGGCVGA QHDSSGSLNE NSEGTGVALG RNQPLKKEKP KWKSDYPMTD GQLRSKRDEF WDTAPAFEGR KEIWDALKAA AHAFESNDHE LAQAIIDGAN ITLPHGALTE CYDELGNRYQ LPVYCLAPPI NMIEEKSDIE TLDIPEPPPN SGYECQLRLR LSTGKDLKLV VRSTDTVFHM KRRLHAAEGV EPGSQRWFFS GRPLTDKMKF EELKIPKDYV VQVIVSQPVQ NPTPVEN

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

Description:

Persephin Human Recombinant

Persephin, PSP, PSPN.

Product # :

CYT-801

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Description

PSPN Human Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.5kDa. The PSPN is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 10ng/ml, corresponding to a specific activity of > 1.0 × 100,000 IU/mg.

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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
Synonyms
Persephin, PSP, PSPN.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PSPN in 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALSGPCQLWS LTLSVAELGL GYASEEKVIF RYCAGSCPRG ARTQHGLALA RLQGQGRAHG GPCCRPTRYT DVAFLDDRHR WQRLPQLSAA ACGCGG.

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

Description:

Interferon-Alpha 2b Human Recombinant, Yeast

Interferon alpha 2b, IFNA, INFA2, IFN-? 2b, MGC125764, MGC125765.

Product # :

CYT-460

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Quantity :

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Shipped at Room temp

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Description

Interferon-alpha 2b Human Recombinant produced in yeast is a single, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of approximately 19.3 kDa.The IFN-a 2b is purified by proprietary chromatographic techniques.

Source

Saccharomyces cerevisiae.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH-7.4 and 0.02% Tween-20.

Purity

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

Biological Activity

The specific activity as determined by an anti-viral assay was found to be no less than 1.6 x10⁸IU/mg.

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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
Interferon alpha 2b, IFNA, INFA2, IFN-? 2b, MGC125764, MGC125765.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized glycosilated IFN-a 2b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized glycosilated IFN alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.
Background
What is the molecular weight/Mw of IFN A 2B HUMAN, YEAST Protein?
IFN A 2B HUMAN, YEAST Protein has a total Mw of 19.3kDa.

What is the source or expression system of IFN A 2B HUMAN, YEAST Protein?
Saccharomyces cerevisiae.

What is the Purity of IFN A 2B HUMAN, YEAST Protein?
IFN A 2B HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2B HUMAN, YEAST Protein?
The specific activity as determined by an anti-viral assay was found to be no less than 1.6 x108IU/mg.

What is the amino acid sequence of IFN A 2B HUMAN, YEAST Protein?
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

What applications can IFN A 2B HUMAN, YEAST Protein be used in?
IFN A 2B HUMAN, YEAST Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2B HUMAN, YEAST Protein?
The endotoxin level is minimal, IFN A 2B HUMAN, YEAST Protein was purified using conventional chromatography techniques.

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Description:

Hepatitis B Surface Antigen, adw2 Recombinant

Product # :

HBS-885

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Description

HbsAg subtype adw2 produced in E.Coli, is a single, non-glycosylated, polypeptide chain containing 226 amino acids and having a molecular weight of approximately 23.0kDa. HBsAg adw2 migrates on SDS-PAGE as a 23kDa monomer band with minor amounts of dimer (46kDa) and trimer (69kDa) forms.The HBsAg is fused to a 6 His tag on C-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Sterile filtered solution containing 50mM potassium phosphate.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNH
SPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGP
CKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFV
QWFVGLSPTVWLSAIWMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI

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Description:

IFN-Alpha 2b Human Recombinant

IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

Product # :

CYT-205

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Description

IFN-a 2b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids and having a molecular mass of 19400 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine. The IFN-alpha 2b gene was obtained from human leukocytes. The IFN-a 2b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN alpha 2b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IFN-alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
Background
IFN-alpha forms are produced by monocytes/macrophages, lymphoblastoid cells, fibroblasts, and a number of different cell types following induction by viruses, nucleic acids, glucocorticoid hormones, and low-molecular weight substances (n-butyrate, 5-bromodeoxy uridine). At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. Disulfide bonds are formed between cysteines at positions 1/98 and 29/138. The disulfide bond 29/138 is essential for biological activity while the 1/98 bond can be reduces without affecting biological activity. All IFN-alpha forms contain a potential glycosylation site but most subtypes are not glycosylated. In contrast to IFN-gamma IFN-alpha proteins are stable at pH2.
There are at least 23 different IFN-alpha genes. They have a length of 1-2 kb and are clustered on human chromosome 9p22. It is not known whether all these genes are expressed following stimulation of the cells. In some cell systems expression of some subtypes (IFN-alpha-1, IFN-alpha-2, IFN-alpha-4) is stronger than those of others. IFN-alpha genes do not contain intron sequences found in many other eukaryotic genes (see also: gene expression). Based upon the structures two types of IFN-alpha genes, designated class 1 and II, are distinguished. They encode proteins of 156-166 and172 amino acids, respectively. Deletions covering 9p22 are observed frequently in cells of lymphoblastoid leukemias. It is not known to date whether this is of significance with respect to IFN expression.
The gene encoding the IFN-alpha receptor maps to human chromosome 21q22.1. IFN-alpha and IFN-beta are thought to bind to the same IFN binding subunit which is expressed in 100-5000 copies in IFN-alpha sensitive and -resistant cells and is associated with other as yet unidentified proteins. The IFN-omega (Omega IFN) also binds to the IFN-alpha/IFN-beta receptor. Another receptor expressed on B-lymphocytes is identical with CD21. This receptor also binds Epstein-Barr virus through its gp350/220 coat protein.Signal transduction mechanisms elicited after binding of IFN-alpha to its receptors involves tyrosine phosphorylation (see also: PTK; protein tyrosine kinase) of various non-receptor tyrosine kinases belonging to the Janus kinases. Soluble forms of the IFN-alpha receptor, corresponding to truncated forms of the extracellular domain of the cell surface IFN-alpha receptor, have been found in human serum and in normal human urine.
All known subtypes of IFN-alpha show the same antiviral antiparasitic, antiproliferative activities in suitable bioassays although they may differ in relative activities. Human IFN-alpha is also a potent antiviral substance in murine, porcine, and bovine cell systems. Human IFN-alpha is less active in rodent cells. Site-directed mutagenesis techniques have been used to create some variants of certain subtypes (IFN-alpha-2) that display approximately 100-fold enhanced antiviral activities in mouse cells.
What is the molecular weight/Mw of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein has a total Mw of 19.4kDa.

What is the source or expression system of IFN A 2B HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2B HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

What is the amino acid sequence of IFN A 2B HUMAN Protein?
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
What applications can IFN A 2B HUMAN Protein be used in?
IFN A 2B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2B HUMAN Protein?
The endotoxin level is minimal, IFN A 2B HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.924 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 by RP-HPLC, using a calibrated solution of IFN alpha 2b as a Reference Standard.

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Description:

Recombinant Human Anti Vascular Endothelial Growth Factor

Product # :

ANT-601

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Description

Recombinant Human Anti Vascular Endothelial Growth Factor that binds to and inhibits the biologic activity of human VEGF in vitro. Recombinant VEGF Antibody contains human framework regions and the complementarity-determining regions of a murine antibody that binds to VEGF. Recombinant VEGF Antibody is produced in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 149 kDa.

Source

CHO.

Formulation

The protein 25.7mg/ml solution contains 60 mg/ml of a,a-trehalose dihydrate, 5.8 mg/ml of sodium phosphate (monobasic, monohydrate), 1.2 mg/ml of sodium phosphate (dibasic, anhydrous) and 0.4 mg/ml of polysorbate 20, pH-6.

Purity

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

Biological Activity

The ED₅₀ as determined by the proliferation inhibition of HUVEC cell, Perform a comparison of a dilution series of the Sample solution with a dilution series of the Standard solution, measured potency was found to be 1.1 X 10⁴EU/mg.

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Introduction
Vascular endothelial growth factoris an important signaling proteininvolved in both vasculogenesisand angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Physical Appearance
Clear, colorless solution.
Stability
Recombinant VEGF Antibody should be stored between 2-8°C and should be protected from light. DO NOT FREEZE.
Amino Acid Sequence
LIGHT CHAIN:
DIQMTQSPSS LSASVGDRVT ITCSASQDIS NYLNWYQQKP GKAPKVLIYF TSSLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ YSTVPWTFGQ GTKVEIKRTV AAPSVFIFPP SDEQLKSGTA SVVCLLNNFY PREAKVQWKV DNALQSGNSQ ESVTEQDSKD STYSLSSTLT LSKADYEKHK VYACEVTHQG LSSPVTKSFN
RGEC.

HEAVY CHAIN:
EVQLVESGGG LVQPGGSLRL SCAASGYTFT NYGMNWVRQA PGKGLEWVGW INTYTGEPTY AADFKRRFTF SLDTSKSTAY LQMNSLRAED TAVYYCAKYP HYYGSSHWYF DVWGQGTLVT VSSASTKGPS VFPLAPSSKS TSGGTAALGC LVKDYFPEPV TVSWNSGALT SGVHTFPAVL QSSGLYSLSS VVTVPSSSLG TQTYICNVNH KPSNTKVDKK VEPKSCDKTH TCPPCPAPEL
LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS REEMTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS
PGK.

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Description:

Mouse Anti Human Ubiquitin Aldehyde Binding 2

Ubiquitin thioesterase OTUB2, Deubiquitinating enzyme OTUB2, OTU domain-containing ubiquitin aldehyde-binding protein 2, Otubain-2, Ubiquitin-specific-processing protease OTUB2, OTUB2, C14orf137, OTB2, OTU2.

Product # :

ANT-743

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Ubiquitin thioesterase OTUB2 (OTUB2) is a member of the peptidase C65 family. OTUB2 functions as a hydrolase which can remove conjugated ubiquitin from proteins in vitro and may thus play a key regulatory role at the level of protein turnover by preventing degradation.
Synonyms
Ubiquitin thioesterase OTUB2, Deubiquitinating enzyme OTUB2, OTU domain-containing ubiquitin aldehyde-binding protein 2, Otubain-2, Ubiquitin-specific-processing protease OTUB2, OTUB2, C14orf137, OTB2, OTU2.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human OTUB2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human OTUB2 protein 1-234 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT1F8AT.
Applications
OTUB2 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
OTUB2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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Description:

Vimentin PAT5H8AT, Mouse Anti Human

Vimentin, Vim, FLJ36605.

Product # :

ANT-682

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
Synonyms
Vimentin, Vim, FLJ36605.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human Vimentin mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human Vimentin protein 1-466 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT5H8AT.
Applications
Vimentin antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
Vimentin antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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Description:

Cystatin 5 Human Recombinant

Cystatin-D, CST5, Cystatin 5, Cystatin-5.

Product # :

PRO-2221

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Description

CST5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 123 amino acids (26-142 a.a) and having a molecular mass of 14.36kDa. CST5 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The CST5 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The IC50 value is < 2.0nM. The inhibitory function of Cystatin 5 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.

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Introduction
Cystatin 5 (CST5) is a novel member of the cystatin superfamily, which encompasses proteins that contain multiple cystatin-like sequences. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions.
Synonyms
Cystatin-D, CST5, Cystatin 5, Cystatin-5.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QSRTLAGGIH ATDLNDKSVQ RALDFAISEY NKVINKDEYY SRPLQVMAAY QQIVGGVNYY FNVKFGRTTC TKSQPNLDNC PFNDQPKLKE EEFCSFQINE VPWEDKISIL NYKCRKVHHH HHH.

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Description:

Cystatin E/M, BioActive Human Recombinant

Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.

Product # :

PRO-2633

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Description

CST6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149 a.a.) and having a molecular mass of 15.9kDa.CST6 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CST6 solution (0.5mg/1ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The IC50 value is < 10nM. The inhibitory function of Cystatin 6 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25˚C.

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Introduction
Cystatin E/M or CST6 is part of the cystatin type 2 family. Part of the cystatin type 2 family members can act as cysteine protease inhibitors, whereas cystatin E/M regulates cathepsin B inhibitors and not cathepsin C. cystatin E/M is a protein the when secreted, has an effect on osteogenesis and bone resorption, insulin regulation, response to systemic inflammation & hepatocyte growth factor receptors.
Synonyms
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM

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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